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1. Generating parallel representations of position and identity in the olfactory system

Author

István Taisz, Erika Donà, Daniel Münch, Shanice N. Bailey, Billy J. Morris, Kimberly I. Meechan, Katie M. Stevens, Irene Varela, Marina Gkantia, Philipp Schlegel, Carlos Ribeiro, Gregory S.X.E. Jefferis, and Dana S. Galili

Subjects
History, Polymers and Plastics, Business and International Management, Industrial and Manufacturing Engineering, General Biochemistry, Genetics and Molecular Biology
Abstract

SummarySex pheromones are key social signals in most animals. In Drosophila a dedicated olfactory channel senses a male pheromone, cis-vaccenyl acetate (cVA) that promotes female courtship while repelling males. Here we show that flies use separate cVA processing streams to extract qualitative and positional information. cVA olfactory neurons are sensitive to concentration differences in a 5 mm range around a male. Second-order projection neurons detect inter-antennal differences in cVA concentration, encoding the angular position of a male. We identify a circuit mechanism increasing left-right contrast through an interneuron which provides contralateral inhibition. At the third layer of the circuit we identify neurons with distinct response properties and sensory integration motifs. One population is selectively tuned to an approaching male with speed-dependent responses. A second population responds tonically to a male’s presence and controls female mating decisions. A third population integrates a male taste cue with cVA; only a simultaneous presentation of both signals promotes female mating via this pathway. Thus the olfactory system generates a range of complex percepts in discrete populations of central neurons that allow the expression of appropriate behaviors depending on context. Such separation of olfactory features resembles the mammalian what and where visual streams.HighlightscVA male pheromone has a 5 mm signaling range, activating two parallel central pathwaysPheromone-sensing neurons have spatial receptive fields sharpened by contralateral inhibitionPosition (where) and identity (what) are separated at the 3rd layer of cVA processingIntegrating taste and cVA in sexually dimorphic aSP-g controls female receptivity

Published
2023
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2. Connectomics and the neural basis of behaviour

Author

Dana S Galili, Gregory SXE Jefferis, Marta Costa, Mesquita da Costa, Marta [0000-0001-5948-3092], and Apollo - University of Cambridge Repository

Subjects
Neurons, Smell, Insect Science, Connectome, Animals, Nervous System, Ecology, Evolution, Behavior and Systematics
Abstract

For the purpose of open access, the authors have applied a Creative Commons Attribution (CC BY) licence to this Author Accepted Manuscript version., Methods to acquire and process synaptic-resolution electron-microscopy datasets have progressed very rapidly, allowing production and annotation of larger, more complete connectomes. More accurate neuronal matching techniques are enriching cell type data with gene expression, neuron activity, behaviour and developmental information, providing ways to test hypotheses of circuit function. In a variety of behaviours such as learned and innate olfaction, navigation and sexual behaviour, connectomics has already revealed interconnected modules with a hierarchical structure, recurrence and integration of sensory streams. Comparing individual connectomes to determine which circuit features are robust and which are variable is one key research area; new work in comparative connectomics across development, experience, sex and species will establish strong links between neuronal connectivity and brain function.

Published
2022

3. Trace conditioning in insects – Keep the trace!

Author

Kristina V Dylla, Dana S Galili, Paul eSzyszka, and Alja eLüdke

Subjects
Insects, Learning, trace conditioning, Olfaction, Stimulus trace, Physiology, QP1-981
Abstract

Trace conditioning is a form of associative learning that can be induced by presenting a conditioned stimulus (CS) and an unconditioned stimulus (US) following each other, but separated by a temporal gap. This gap distinguishes trace conditioning from classical delay conditioning, where the CS and US overlap. To bridge the temporal gap between both stimuli and to form an association between CS and US in trace conditioning, the brain must keep a neural representation of the CS after its termination – a stimulus trace. Behavioral and physiological studies on trace and delay conditioning revealed similarities between the two forms of learning, like similar memory decay and similar odor identity perception in invertebrates. On the other hand differences were reported also, like the requirement of distinct brain structures in vertebrates or disparities in molecular mechanisms in both vertebrates and invertebrates. For example, in commonly used vertebrate conditioning paradigms the hippocampus is necessary for trace but not for delay conditioning, and Drosophila delay conditioning requires the Rutabaga adenylyl cyclase, which is dispensable in trace conditioning. It is still unknown how the brain encodes CS traces and how they are associated with a US in trace conditioning. Insects serve as powerful models to address the mechanisms underlying trace conditioning, due to their simple brain anatomy, behavioral accessibility and established methods of genetic interference. In this review we summarize the recent progress in insect trace conditioning on the behavioral and physiological level and emphasize similarities and differences compared to delay conditioning. Moreover, we examine proposed molecular and computational models and reassess different experimental approaches used for trace conditioning.

Published
2013
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4. Behavior: Why Male Flies Sing Different Songs

Author

Dana S. Galili and Gregory S.X.E. Jefferis

Subjects
Male, 0301 basic medicine, animal structures, media_common.quotation_subject, Biology, General Biochemistry, Genetics and Molecular Biology, Courtship, Sexual Behavior, Animal, 03 medical and health sciences, 0302 clinical medicine, Downstream (manufacturing), Motor system, Animals, Drosophila, media_common, Neurons, fungi, Brain, biology.organism_classification, 030104 developmental biology, nervous system, Sexual behavior, Evolutionary biology, behavior and behavior mechanisms, Evolutionary divergence, General Agricultural and Biological Sciences, psychological phenomena and processes, 030217 neurology & neurosurgery
Abstract

A new study investigates the distinct male courtship songs of two related Drosophila species and the neurons controlling this behavior, localizing a site of evolutionary divergence to the motor system, downstream of the central brain.

Published
2019
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5. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Author

Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. Bhutia, S.K. Biagosch, C. Bianchi, M.W. Biard-Piechaczyk, M. Billes, V. Bincoletto, C. Bingol, B. Bird, S.W. Bitoun, M. Bjedov, I. Blackstone, C. Blanc, L. Blanco, G.A. Blomhoff, H.K. Boada-Romero, E. Böckler, S. Boes, M. Boesze-Battaglia, K. Boise, L.H. Bolino, A. Boman, A. Bonaldo, P. Bordi, M. Bosch, J. Botana, L.M. Botti, J. Bou, G. Bouché, M. Bouchecareilh, M. Boucher, M.-J. Boulton, M.E. Bouret, S.G. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N. Braga, V.M.M. Brancolini, C. Braus, G.H. Bravo-San-Pedro, J.M. Brennan, L.A. Bresnick, E.H. Brest, P. Bridges, D. Bringer, M.-A. Brini, M. Brito, G.C. Brodin, B. Brookes, P.S. Brown, E.J. Brown, K. Broxmeyer, H.E. Bruhat, A. Brum, P.C. Brumell, J.H. Brunetti-Pierri, N. Bryson-Richardson, R.J. Buch, S. Buchan, A.M. Budak, H. Bulavin, D.V. Bultman, S.J. Bultynck, G. Bumbasirevic, V. Burelle, Y. Burke, R.E. Burmeister, M. Bütikofer, P. Caberlotto, L. Cadwell, K. Cahova, M. Cai, D. Cai, J. Cai, Q. Calatayud, S. Camougrand, N. Campanella, M. Campbell, G.R. Campbell, M. Campello, S. Candau, R. Caniggia, I. Cantoni, L. Cao, L. Caplan, A.B. Caraglia, M. Cardinali, C. Cardoso, S.M. Carew, J.S. Carleton, L.A. Carlin, C.R. Carloni, S. Carlsson, S.R. Carmona-Gutierrez, D. Carneiro, L.A.M. Carnevali, O. Carra, S. Carrier, A. Carroll, B. Casas, C. Casas, J. Cassinelli, G. Castets, P. Castro-Obregon, S. Cavallini, G. Ceccherini, I. Cecconi, F. Cederbaum, A.I. Ceña, V. Cenci, S. Cerella, C. Cervia, D. Cetrullo, S. Chaachouay, H. Chae, H.-J. Chagin, A.S. Chai, C.-Y. Chakrabarti, G. Chamilos, G. Chan, E.Y.W. Chan, M.T.V. Chandra, D. Chandra, P. Chang, C.-P. Chang, R.C.-C. Chang, T.Y. Chatham, J.C. Chatterjee, S. Chauhan, S. Che, Y. Cheetham, M.E. Cheluvappa, R. Chen, C.-J. Chen, G. Chen, G.-C. Chen, G. Chen, H. Chen, J.W. Chen, J.-K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S.-D. Chen, S. Chen, S.S.-L. Chen, W. Chen, W.-J. Chen, W.Q. Chen, W. Chen, X. Chen, Y.-H. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Y.-Q. Chen, Y. Chen, Z. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, H. Cheong, H. Cherry, S. Chesney, J. Cheung, C.H.A. Chevet, E. Chi, H.C. Chi, S.-G. Chiacchiera, F. Chiang, H.-L. Chiarelli, R. Chiariello, M. Chieppa, M. Chin, L.-S. Chiong, M. Chiu, G.N.C. Cho, D.-H. Cho, S.-G. Cho, W.C. Cho, Y.-Y. Cho, Y.-S. Choi, A.M.K. Choi, E.-J. Choi, E.-K. Choi, J. Choi, M.E. Choi, S.-I. Chou, T.-F. Chouaib, S. Choubey, D. Choubey, V. Chow, K.-C. Chowdhury, K. Chu, C.T. Chuang, T.-H. Chun, T. Chung, H. Chung, T. Chung, Y.-L. Chwae, Y.-J. Cianfanelli, V. Ciarcia, R. Ciechomska, I.A. Ciriolo, M.R. Cirone, M. Claerhout, S. Clague, M.J. Cl� ria, J. Clarke, P.G.H. Clarke, R. Clementi, E. Cleyrat, C. Cnop, M. Coccia, E.M. Cocco, T. Codogno, P. Coers, J. Cohen, E.E.W. Colecchia, D. Coletto, L. Coll, N.S. Colucci-Guyon, E. Comincini, S. Condello, M. Cook, K.L. Coombs, G.H. Cooper, C.D. Cooper, J.M. Coppens, I. Corasaniti, M.T. Corazzari, M. Corbalan, R. Corcelle-Termeau, E. Cordero, M.D. Corral-Ramos, C. Corti, O. Cossarizza, A. Costelli, P. Costes, S. Cotman, S.L. Coto-Montes, A. Cottet, S. Couve, E. Covey, L.R. Cowart, L.A. Cox, J.S. Coxon, F.P. Coyne, C.B. Cragg, M.S. Craven, R.J. Crepaldi, T. Crespo, J.L. Criollo, A. Crippa, V. Cruz, M.T. Cuervo, A.M. Cuezva, J.M. Cui, T. Cutillas, P.R. Czaja, M.J. Czyzyk-Krzeska, M.F. Dagda, R.K. Dahmen, U. Dai, C. Dai, W. Dai, Y. Dalby, K.N. Valle, L.D. Dalmasso, G. D'amelio, M. Damme, M. Darfeuille-Michaud, A. Dargemont, C. Darley-Usmar, V.M. Dasarathy, S. Dasgupta, B. Dash, S. Dass, C.R. Davey, H.M. Davids, L.M. Dávila, D. Davis, R.J. Dawson, T.M. Dawson, V.L. Daza, P. de Belleroche, J. de Figueiredo, P. de Figueiredo, R.C.B.Q. de la Fuente, J. De Martino, L. De Matteis, A. De Meyer, G.R.Y. De Milito, A. De Santi, M. de Souza, W. De Tata, V. De Zio, D. Debnath, J. Dechant, R. Decuypere, J.-P. Deegan, S. Dehay, B. Del Bello, B. Del Re, D.P. Delage-Mourroux, R. Delbridge, L.M.D. Deldicque, L. Delorme-Axford, E. Deng, Y. Dengjel, J. Denizot, M. Dent, P. Der, C.J. Deretic, V. Derrien, B. Deutsch, E. Devarenne, T.P. Devenish, R.J. Di Bartolomeo, S. Di Daniele, N. Di Domenico, F. Di Nardo, A. Di Paola, S. Di Pietro, A. Di Renzo, L. Di Antonio, A. Díaz-Araya, G. Díaz-Laviada, I. Diaz-Meco, M.T. Diaz-Nido, J. Dickey, C.A. Dickson, R.C. Diederich, M. Digard, P. Dikic, I. Dinesh-Kumar, S.P. Ding, C. Ding, W.-X. Ding, Z. Dini, L. Distler, J.H.W. Diwan, A. Djavaheri-Mergny, M. Dmytruk, K. Dobson, R.C.J. Doetsch, V. Dokladny, K. Dokudovskaya, S. Donadelli, M. Dong, X.C. Dong, X. Dong, Z. Donohue, T.M., Jr. Donohue-Jr, T.M. Doran, K.S. D'orazi, G. Dorn, G.W., II Dosenko, V. Dridi, S. Drucker, L. Du, J. Du, L.-L. Du, L. du Toit, A. Dua, P. Duan, L. Duann, P. Dubey, V.K. Duchen, M.R. Duchosal, M.A. Duez, H. Dugail, I. Dumit, V.I. Duncan, M.C. Dunlop, E.A. Dunn, W.A., Jr. Dupont, N. Dupuis, L. Durán, R.V. Durcan, T.M. Duvezin-Caubet, S. Duvvuri, U. Eapen, V. Ebrahimi-Fakhari, D. Echard, A. Eckhart, L. Edelstein, C.L. Edinger, A.L. Eichinger, L. Eisenberg, T. Eisenberg-Lerner, A. Eissa, N.T. El-Deiry, W.S. El-Khoury, V. Elazar, Z. Eldar-Finkelman, H. Elliott, C.J.H. Emanuele, E. Emmenegger, U. Engedal, N. Engelbrecht, A.-M. Engelender, S. Enserink, J.M. Erdmann, R. Erenpreisa, J. Eri, R. Eriksen, J.L. Erman, A. Escalante, R. Eskelinen, E.-L. Espert, L. Esteban-Martínez, L. Evans, T.J. Fabri, M. Fabrias, G. Fabrizi, C. Facchiano, A. Færgeman, N.J. Faggioni, A. Fairlie, W.D. Fan, C. Fan, D. Fan, J. Fang, S. Fanto, M. Fanzani, A. Farkas, T. Faure, M. Favier, F.B. Fearnhead, H. Federici, M. Fei, E. Felizardo, T.C. Feng, H. Feng, Y. Feng, Y. Ferguson, T.A. Fernández, Á.F. Fernandez-Barrena, M.G. Fernandez-Checa, J.C. Fernández-López, A. Fernandez-Zapico, M.E. Feron, O. Ferraro, E. Ferreira-Halder, C.V. Fesus, L. Feuer, R. Fiesel, F.C. Filippi-Chiela, E.C. Filomeni, G. Fimia, G.M. Fingert, J.H. Finkbeiner, S. Finkel, T. Fiorito, F. Fisher, P.B. Flajolet, M. Flamigni, F. Florey, O. Florio, S. Floto, R.A. Folini, M. Follo, C. Fon, E.A. Fornai, F. Fortunato, F. Fraldi, A. Franco, R. Francois, A. François, A. Frankel, L.B. Fraser, I.D.C. Frey, N. Freyssenet, D.G. Frezza, C. Friedman, S.L. Frigo, D.E. Fu, D. Fuentes, J.M. Fueyo, J. Fujitani, Y. Fujiwara, Y. Fujiya, M. Fukuda, M. Fulda, S. Fusco, C. Gabryel, B. Gaestel, M. Gailly, P. Gajewska, M. Galadari, S. Galili, G. Galindo, I. Galindo, M.F. Galliciotti, G. Galluzzi, L. Galluzzi, L. Galy, V. Gammoh, N. Gandy, S. Ganesan, A.K. Ganesan, S. Ganley, I.G. Gannagé, M. Gao, F.-B. Gao, F. Gao, J.-X. Nannig, L.G. Véscovi, E.G. Garcia-Macía, M. Garcia-Ruiz, C. Garg, A.D. Garg, P.K. Gargini, R. Gassen, N.C. Gatica, D. Gatti, E. Gavard, J. Gavathiotis, E. Ge, L. Ge, P. Ge, S. Gean, P.-W. Gelmetti, V. Genazzani, A.A. Geng, J. Genschik, P. Gerner, L. Gestwicki, J.E. Gewirtz, D.A. Ghavami, S. Ghigo, E. Ghosh, D. Giammarioli, A.M. Giampieri, F. Giampietri, C. Giatromanolaki, A. Gibbings, D.J. Gibellini, L. Gibson, S.B. Ginet, V. Giordano, A. Giorgini, F. Giovannetti, E. Girardin, S.E. Gispert, S. Giuliano, S. Gladson, C.L. Glavic, A. Gleave, M. Godefroy, N. Gogal, R.M., Jr. Gokulan, K. Goldman, G.H. Goletti, D. Goligorsky, M.S. Gomes, A.V. Gomes, L.C. Gomez, H. Gomez-Manzano, C. Gómez-Sánchez, R. Gonçalves, D.A.P. Goncu, E. Gong, Q. Gongora, C. Gonzalez, C.B. Gonzalez-Alegre, P. Gonzalez-Cabo, P. González-Polo, R.A. Goping, I.S. Gorbea, C. Gorbunov, N.V. Goring, D.R. Gorman, A.M. Gorski, S.M. Goruppi, S. Goto-Yamada, S. Gotor, C. Gottlieb, R.A. Gozes, I. Gozuacik, D. Graba, Y. Graef, M. Granato, G.E. Grant, G.D. Grant, S. Gravina, G.L. Green, D.R. Greenhough, A. Greenwood, M.T. Grimaldi, B. Gros, F. Grose, C. Groulx, J.-F. Gruber, F. Grumati, P. Grune, T. Guan, J.-L. Guan, K.-L. Guerra, B. Guillen, C. Gulshan, K. Gunst, J. Guo, C. Guo, L. Guo, M. Guo, W. Guo, X.-G. Gust, A.A. Gustafsson, Å.B. Gutierrez, E. Gutierrez, M.G. Gwak, H.-S. Haas, A. Haber, J.E. Hadano, S. Hagedorn, M. Hahn, D.R. Halayko, A.J. Hamacher-Brady, A. Hamada, K. Hamai, A. Hamann, A. Hamasaki, M. Hamer, I. Hamid, Q. Hammond, E.M. Han, F. Han, W. Handa, J.T. Hanover, J.A. Hansen, M. Harada, M. Harhaji-Trajkovic, L. Harper, J.W. Harrath, A.H. Harris, A.L. Harris, J. Hasler, U. Hasselblatt, P. Hasui, K. Hawley, R.G. Hawley, T.S. He, C. He, C.Y. He, F. He, G. He, R.-R. He, X.-H. He, Y.-W. He, Y.-Y. Heath, J.K. Hébert, M.-J. Heinzen, R.A. Helgason, G.V. Hensel, M. Henske, E.P. Her, C. Herman, P.K. Hernández, A. Hernandez, C. Hernández-Tiedra, S. Hetz, C. Hiesinger, P.R. Higaki, K. Hilfiker, S. Hill, B.G. Hill, J.A. Hill, W.D. Hino, K. Hofius, D. Hofman, P. Höglinger, G.U. Höhfeld, J. Holz, M.K. Hong, Y. Hood, D.A. Hoozemans, J.J.M. Hoppe, T. Hsu, C. Hsu, C.-Y. Hsu, L.-C. Hu, D. Hu, G. Hu, H.-M. Hu, H. Hu, M.C. Hu, Y.-C. Hu, Z.-W. Hua, F. Hua, Y. Huang, C. Huang, H.-L. Huang, K.-H. Huang, K.-Y. Huang, S. Huang, S. Huang, W.-P. Huang, Y.-R. Huang, Y. Huang, Y. Huber, T.B. Huebbe, P. Huh, W.-K. Hulmi, J.J. Hur, G.M. Hurley, J.H. Husak, Z. Hussain, S.N.A. Hussain, S. Hwang, J.J. Hwang, S. Hwang, T.I.S. Ichihara, A. Imai, Y. Imbriano, C. Inomata, M. Into, T. Iovane, V. Iovanna, J.L. Iozzo, R.V. Ip, N.Y. Irazoqui, J.E. Iribarren, P. Isaka, Y. Isakovic, A.J. Ischiropoulos, H. Isenberg, J.S. Ishaq, M. Ishida, H. Ishii, I. Ishmael, J.E. Isidoro, C. Isobe, K.-I. Isono, E. Issazadeh-Navikas, S. Itahana, K. Itakura, E. Ivanov, A.I. Iyer, A.K.V. Izquierdo, J.M. Izumi, Y. Izzo, V. Jäättelä, M. Jaber, N. Jackson, D.J. Jackson, W.T. Jacob, T.G. Jacques, T.S. Jagannath, C. Jain, A. Jana, N.R. Jang, B.K. Jani, A. Janji, B. Jannig, P.R. Jansson, P.J. Jean, S. Jendrach, M. Jeon, J.-H. Jessen, N. Jeung, E.-B. Jia, K. Jia, L. Jiang, H. Jiang, H. Jiang, L. Jiang, T. Jiang, X. Jiang, X. Jiang, Y. Jiang, Y. Jiménez, A. Jin, C. Jin, H. Jin, L. Jin, M. Jin, S. Jinwal, U.K. Jo, E.-K. Johansen, T. Johnson, D.E. Johnson, G.V.W. Johnson, J.D. Jonasch, E. Jones, C. Joosten, L.A.B. Jordan, J. Joseph, A.-M. Joseph, B. Joubert, A.M. Ju, D. Ju, J. Juan, H.-F. Juenemann, K. Juhász, G. Jung, H.S. Jung, J.U. Jung, Y.-K. Jungbluth, H. Justice, M.J. Jutten, B. Kaakoush, N.O. Kaarniranta, K. Kaasik, A. Kabuta, T. Kaeffer, B. Kågedal, K. Kahana, A. Kajimura, S. Kakhlon, O. Kalia, M. Kalvakolanu, D.V. Kamada, Y. Kambas, K. Kaminskyy, V.O. Kampinga, H.H. Kandouz, M. Kang, C. Kang, R. Kang, T.-C. Kanki, T. Kanneganti, T.-D. Kanno, H. Kanthasamy, A.G. Kantorow, M. Kaparakis-Liaskos, M. Kapuy, O. Karantza, V. Karim, M.R. Karmakar, P. Kaser, A. Kaushik, S. Kawula, T. Kaynar, A.M. Ke, P.-Y. Ke, Z.-J. Kehrl, J.H. Keller, K.E. Kemper, J.K. Kenworthy, A.K. Kepp, O. Kern, A. Kesari, S. Kessel, D. Ketteler, R. Kettelhut, I.C. Khambu, B. Khan, M.M. Khandelwal, V.K.M. Khare, S. Kiang, J.G. Kiger, A.A. Kihara, A. Kim, A.L. Kim, C.H. Kim, D.R. Kim, D.-H. Kim, E.K. Kim, H.Y. Kim, H.-R. Kim, J.-S. Kim, J.H. Kim, J.C. Kim, J.H. Kim, K.W. Kim, M.D. Kim, M.-M. Kim, P.K. Kim, S.W. Kim, S.-Y. Kim, Y.-S. Kim, Y. Kimchi, A. 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Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.

Published
2016

6. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author

Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. Bhutia, S.K. Biagosch, C. Bianchi, M.W. Biard-Piechaczyk, M. Billes, V. Bincoletto, C. Bingol, B. Bird, S.W. Bitoun, M. Bjedov, I. Blackstone, C. Blanc, L. Blanco, G.A. Blomhoff, H.K. Boada-Romero, E. Böckler, S. Boes, M. Boesze-Battaglia, K. Boise, L.H. Bolino, A. Boman, A. Bonaldo, P. Bordi, M. Bosch, J. Botana, L.M. Botti, J. Bou, G. Bouché, M. Bouchecareilh, M. Boucher, M.-J. Boulton, M.E. Bouret, S.G. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N. Braga, V.M.M. Brancolini, C. Braus, G.H. Bravo-San-Pedro, J.M. Brennan, L.A. Bresnick, E.H. Brest, P. Bridges, D. Bringer, M.-A. Brini, M. Brito, G.C. Brodin, B. Brookes, P.S. Brown, E.J. Brown, K. Broxmeyer, H.E. Bruhat, A. Brum, P.C. Brumell, J.H. Brunetti-Pierri, N. Bryson-Richardson, R.J. Buch, S. Buchan, A.M. Budak, H. Bulavin, D.V. Bultman, S.J. Bultynck, G. Bumbasirevic, V. Burelle, Y. Burke, R.E. Burmeister, M. Bütikofer, P. Caberlotto, L. Cadwell, K. Cahova, M. Cai, D. Cai, J. Cai, Q. Calatayud, S. Camougrand, N. Campanella, M. Campbell, G.R. Campbell, M. Campello, S. Candau, R. Caniggia, I. Cantoni, L. Cao, L. Caplan, A.B. Caraglia, M. Cardinali, C. Cardoso, S.M. Carew, J.S. Carleton, L.A. Carlin, C.R. Carloni, S. Carlsson, S.R. Carmona-Gutierrez, D. Carneiro, L.A.M. Carnevali, O. Carra, S. Carrier, A. Carroll, B. Casas, C. Casas, J. Cassinelli, G. Castets, P. Castro-Obregon, S. Cavallini, G. Ceccherini, I. Cecconi, F. Cederbaum, A.I. Ceña, V. Cenci, S. Cerella, C. Cervia, D. Cetrullo, S. Chaachouay, H. Chae, H.-J. Chagin, A.S. Chai, C.-Y. Chakrabarti, G. Chamilos, G. Chan, E.Y.W. Chan, M.T.V. Chandra, D. Chandra, P. Chang, C.-P. Chang, R.C.-C. Chang, T.Y. Chatham, J.C. Chatterjee, S. Chauhan, S. Che, Y. Cheetham, M.E. Cheluvappa, R. Chen, C.-J. Chen, G. Chen, G.-C. Chen, G. Chen, H. Chen, J.W. Chen, J.-K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S.-D. Chen, S. Chen, S.S.-L. Chen, W. Chen, W.-J. Chen, W.Q. Chen, W. Chen, X. Chen, Y.-H. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Y.-Q. Chen, Y. Chen, Z. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, H. Cheong, H. Cherry, S. Chesney, J. Cheung, C.H.A. Chevet, E. Chi, H.C. Chi, S.-G. Chiacchiera, F. Chiang, H.-L. Chiarelli, R. Chiariello, M. Chieppa, M. Chin, L.-S. Chiong, M. Chiu, G.N.C. Cho, D.-H. Cho, S.-G. Cho, W.C. Cho, Y.-Y. Cho, Y.-S. Choi, A.M.K. Choi, E.-J. Choi, E.-K. Choi, J. Choi, M.E. Choi, S.-I. Chou, T.-F. Chouaib, S. Choubey, D. Choubey, V. Chow, K.-C. Chowdhury, K. Chu, C.T. Chuang, T.-H. Chun, T. Chung, H. Chung, T. Chung, Y.-L. Chwae, Y.-J. Cianfanelli, V. Ciarcia, R. Ciechomska, I.A. Ciriolo, M.R. Cirone, M. Claerhout, S. Clague, M.J. Clària, J. Clarke, P.G.H. Clarke, R. Clementi, E. Cleyrat, C. Cnop, M. Coccia, E.M. Cocco, T. Codogno, P. Coers, J. Cohen, E.E.W. Colecchia, D. Coletto, L. Coll, N.S. Colucci-Guyon, E. Comincini, S. Condello, M. Cook, K.L. Coombs, G.H. Cooper, C.D. Cooper, J.M. Coppens, I. Corasaniti, M.T. Corazzari, M. Corbalan, R. Corcelle-Termeau, E. Cordero, M.D. Corral-Ramos, C. Corti, O. Cossarizza, A. Costelli, P. Costes, S. Cotman, S.L. Coto-Montes, A. Cottet, S. Couve, E. Covey, L.R. Cowart, L.A. Cox, J.S. Coxon, F.P. Coyne, C.B. Cragg, M.S. Craven, R.J. Crepaldi, T. Crespo, J.L. Criollo, A. Crippa, V. Cruz, M.T. Cuervo, A.M. Cuezva, J.M. Cui, T. Cutillas, P.R. Czaja, M.J. Czyzyk-Krzeska, M.F. Dagda, R.K. Dahmen, U. Dai, C. Dai, W. Dai, Y. Dalby, K.N. Valle, L.D. Dalmasso, G. D'amelio, M. Damme, M. Darfeuille-Michaud, A. Dargemont, C. Darley-Usmar, V.M. Dasarathy, S. Dasgupta, B. Dash, S. Dass, C.R. Davey, H.M. Davids, L.M. Dávila, D. Davis, R.J. Dawson, T.M. Dawson, V.L. Daza, P. de Belleroche, J. de Figueiredo, P. de Figueiredo, R.C.B.Q. de la Fuente, J. De Martino, L. De Matteis, A. De Meyer, G.R.Y. De Milito, A. De Santi, M. de Souza, W. De Tata, V. De Zio, D. Debnath, J. Dechant, R. Decuypere, J.-P. Deegan, S. Dehay, B. Del Bello, B. Del Re, D.P. Delage-Mourroux, R. Delbridge, L.M.D. Deldicque, L. Delorme-Axford, E. Deng, Y. Dengjel, J. Denizot, M. Dent, P. Der, C.J. Deretic, V. Derrien, B. Deutsch, E. Devarenne, T.P. Devenish, R.J. Di Bartolomeo, S. Di Daniele, N. Di Domenico, F. Di Nardo, A. Di Paola, S. Di Pietro, A. Di Renzo, L. Di Antonio, A. Díaz-Araya, G. Díaz-Laviada, I. Diaz-Meco, M.T. Diaz-Nido, J. Dickey, C.A. Dickson, R.C. Diederich, M. Digard, P. Dikic, I. Dinesh-Kumar, S.P. Ding, C. Ding, W.-X. Ding, Z. Dini, L. Distler, J.H.W. Diwan, A. Djavaheri-Mergny, M. Dmytruk, K. Dobson, R.C.J. Doetsch, V. Dokladny, K. Dokudovskaya, S. Donadelli, M. Dong, X.C. Dong, X. Dong, Z. Donohue, T.M., Jr. Donohue-Jr, T.M. Doran, K.S. D'orazi, G. Dorn, G.W., II Dosenko, V. Dridi, S. Drucker, L. Du, J. Du, L.-L. Du, L. du Toit, A. Dua, P. Duan, L. Duann, P. Dubey, V.K. Duchen, M.R. Duchosal, M.A. Duez, H. Dugail, I. Dumit, V.I. Duncan, M.C. Dunlop, E.A. Dunn, W.A., Jr. Dupont, N. Dupuis, L. Durán, R.V. Durcan, T.M. Duvezin-Caubet, S. Duvvuri, U. Eapen, V. Ebrahimi-Fakhari, D. Echard, A. Eckhart, L. Edelstein, C.L. Edinger, A.L. Eichinger, L. Eisenberg, T. Eisenberg-Lerner, A. Eissa, N.T. El-Deiry, W.S. El-Khoury, V. Elazar, Z. Eldar-Finkelman, H. Elliott, C.J.H. Emanuele, E. Emmenegger, U. Engedal, N. Engelbrecht, A.-M. Engelender, S. Enserink, J.M. Erdmann, R. Erenpreisa, J. Eri, R. Eriksen, J.L. Erman, A. Escalante, R. Eskelinen, E.-L. Espert, L. Esteban-Martínez, L. Evans, T.J. Fabri, M. Fabrias, G. Fabrizi, C. Facchiano, A. Færgeman, N.J. Faggioni, A. Fairlie, W.D. Fan, C. Fan, D. Fan, J. Fang, S. Fanto, M. Fanzani, A. Farkas, T. Faure, M. Favier, F.B. Fearnhead, H. Federici, M. Fei, E. Felizardo, T.C. Feng, H. Feng, Y. Feng, Y. Ferguson, T.A. Fernández, Á.F. Fernandez-Barrena, M.G. Fernandez-Checa, J.C. Fernández-López, A. Fernandez-Zapico, M.E. Feron, O. Ferraro, E. Ferreira-Halder, C.V. Fesus, L. Feuer, R. Fiesel, F.C. Filippi-Chiela, E.C. Filomeni, G. Fimia, G.M. Fingert, J.H. Finkbeiner, S. Finkel, T. Fiorito, F. Fisher, P.B. Flajolet, M. Flamigni, F. Florey, O. 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Rogov, V.V. Rohn, T.T. Rohrer, B. Romanelli, D. Romani, L. Romano, P.S. Roncero, M.I.G. Rosa, J.L. Rosello, A. Rosen, K.V. Rosenstiel, P. Rost-Roszkowska, M. Roth, K.A. Roué, G. Rouis, M. Rouschop, K.M. Ruan, D.T. Ruano, D. Rubinsztein, D.C. Rucker, E.B., III Rudich, A. Rudolf, E. Rudolf, R. Ruegg, M.A. Ruiz-Roldan, C. Ruparelia, A.A. Rusmini, P. Russ, D.W. Russo, G.L. Russo, G. Russo, R. Rusten, T.E. Ryabovol, V. Ryan, K.M. Ryter, S.W. Sabatini, D.M. Sacher, M. Sachse, C. Sack, M.N. Sadoshima, J. Saftig, P. Sagi-Eisenberg, R. Sahni, S. Saikumar, P. Saito, T. Saitoh, T. Sakakura, K. Sakoh-Nakatogawa, M. Sakuraba, Y. Salazar-Roa, M. Salomoni, P. Saluja, A.K. Salvaterra, P.M. Salvioli, R. Samali, A. Sanchez, A.M.J. Sánchez-Alcázar, J.A. Sanchez-Prieto, R. Sandri, M. Sanjuan, M.A. Santaguida, S. Santambrogio, L. Santoni, G. Dos Santos, C.N. Saran, S. Sardiello, M. Sargent, G. Sarkar, P. Sarkar, S. Sarrias, M.R. Sarwal, M.M. Sasakawa, C. Sasaki, M. Sass, M. Sato, K. Sato, M. Satriano, J. Savaraj, N. Saveljeva, S. Schaefer, L. Schaible, U.E. Scharl, M. Schatzl, H.M. Schekman, R. Scheper, W. Schiavi, A. Schipper, H.M. Schmeisser, H. Schmidt, J. Schmitz, I. Schneider, B.E. Schneider, E.M. Schneider, J.L. Schon, E.A. Schönenberger, M.J. Schönthal, A.H. Schorderet, D.F. Schröder, B. Schuck, S. Schulze, R.J. Schwarten, M. Schwarz, T.L. Sciarretta, S. Scotto, K. Scovassi, A.I. Screaton, R.A. Screen, M. Seca, H. Sedej, S. Segatori, L. Segev, N. Seglen, P.O. Seguí-Simarro, J.M. Segura-Aguilar, J. Seiliez, I. Seki, E. Sell, C. Semenkovich, C.F. Semenza, G.L. Sen, U. Serra, A.L. Serrano-Puebla, A. Sesaki, H. Setoguchi, T. Settembre, C. Shacka, J.J. Shajahan-Haq, A.N. Shapiro, I.M. Sharma, S. She, H. Shen, C.-K.J. Shen, C.-C. Shen, H.-M. Shen, S. Shen, W. Sheng, R. Sheng, X. Sheng, Z.-H. Shepherd, T.G. Shi, J. Shi, Q. Shi, Q. Shi, Y. Shibutani, S. Shibuya, K. Shidoji, Y. Shieh, J.-J. Shih, C.-M. Shimada, Y. Shimizu, S. Shin, D.W. Shinohara, M.L. Shintani, M. Shintani, T. Shioi, T. Shirabe, K. Shiri-Sverdlov, R. Shirihai, O. Shore, G.C. Shu, C.-W. Shukla, D. Sibirny, A.A. Sica, V. Sigurdson, C.J. Sigurdsson, E.M. Sijwali, P.S. Sikorska, B. Silveira, W.A. Silvente-Poirot, S. Silverman, G.A. Simak, J. Simmet, T. Simon, A.K. Simon, H.-U. Simone, C. Simons, M. Simonsen, A. Singh, R. Singh, S.V. Singh, S.K. Sinha, D. Sinha, S. Sinicrope, F.A. Sirko, A. Sirohi, K. Sishi, B.J.N. Sittler, A. Siu, P.M. Sivridis, E. Skwarska, A. Slack, R. Slaninová, I. Slavov, N. Smaili, S.S. Smalley, K.S.M. Smith, D.R. Soenen, S.J. Soleimanpour, S.A. Solhaug, A. Somasundaram, K. Son, J.H. Sonawane, A. Song, C. Song, F. Song, H.K. Song, J.-X. Song, W. Soo, K.Y. Sood, A.K. Soong, T.W. Soontornniyomkij, V. Sorice, M. Sotgia, F. Soto-Pantoja, D.R. Sotthibundhu, A. Sousa, M.J. Spaink, H.P. Span, P.N. Spang, A. Sparks, J.D. Speck, P.G. Spector, S.A. Spies, C.D. Springer, W. Clair, D.S. Stacchiotti, A. Staels, B. Stang, M.T. Starczynowski, D.T. Starokadomskyy, P. Steegborn, C. Steele, J.W. Stefanis, L. Steffan, J. Stellrecht, C.M. Stenmark, H. Stepkowski, T.M. Stern, S.T. Stevens, C. Stockwell, B.R. Stoka, V. Storchova, Z. Stork, B. Stratoulias, V. Stravopodis, D.J. Strnad, P. Strohecker, A.M. Ström, A.-L. Stromhaug, P. Stulik, J. Su, Y.-X. Su, Z. Subauste, C.S. Subramaniam, S. Sue, C.M. Suh, S.W. Sui, X. Sukseree, S. Sulzer, D. Sun, F.-L. Sun, J. Sun, J. Sun, S.-Y. Sun, Y. Sun, Y. Sun, Y. Sundaramoorthy, V. Sung, J. Suzuki, H. Suzuki, K. Suzuki, N. Suzuki, T. Suzuki, Y.J. Swanson, M.S. Swanton, C. Swärd, K. Swarup, G. Sweeney, S.T. Sylvester, P.W. Szatmari, Z. Szegezdi, E. Szlosarek, P.W. Taegtmeyer, H. Tafani, M. Taillebourg, E. Tait, S.W.G. Takacs-Vellai, K. Takahashi, Y. Takáts, S. Takemura, G. Takigawa, N. Talbot, N.J. Tamagno, E. Tamburini, J. Tan, C.-P. Tan, L. Tan, M.L. Tan, M. Tan, Y.-J. Tanaka, K. Tanaka, M. Tang, D. Tang, D. Tang, G. Tanida, I. Tanji, K. Tannous, B.A. Tapia, J.A. Tasset-Cuevas, I. Tatar, M. Tavassoly, I. Tavernarakis, N. Taylor, A. Taylor, G.S. Taylor, G.A. Taylor, J.P. Taylor, M.J. Tchetina, E.V. Tee, A.R. Teixeira-Clerc, F. Telang, S. Tencomnao, T. Teng, B.-B. Teng, R.-J. Terro, F. Tettamanti, G. Theiss, A.L. Theron, A.E. Thomas, K.J. Thomé, M.P. Thomes, P.G. Thorburn, A. Thorner, J. Thum, T. Thumm, M. Thurston, T.L.M. Tian, L. Till, A. Ting, J.P.-Y. Ting, J.P.Y. Titorenko, V.I. Toker, L. Toldo, S. Tooze, S.A. Topisirovic, I. Torgersen, M.L. Torosantucci, L. Torriglia, A. Torrisi, M.R. Tournier, C. Towns, R. Trajkovic, V. Travassos, L.H. Triola, G. Tripathi, D.N. Trisciuoglio, D. Troncoso, R. Trougakos, I.P. Truttmann, A.C. Tsai, K.-J. Tschan, M.P. Tseng, Y.-H. Tsukuba, T. Tsung, A. Tsvetkov, A.S. Tu, S. Tuan, H.-Y. Tucci, M. Tumbarello, D.A. Turk, B. Turk, V. Turner, R.F.B. Tveita, A.A. Tyagi, S.C. Ubukata, M. Uchiyama, Y. Udelnow, A. Ueno, T. Umekawa, M. Umemiya-Shirafuji, R. Underwood, B.R. Ungermann, C. Ureshino, R.P. Ushioda, R. Uversky, V.N. Uzcátegui, N.L. Vaccari, T. Vaccaro, M.I. Váchová, L. Vakifahmetoglu-Norberg, H. Valdor, R. Valente, E.M. Vallette, F. Valverde, A.M. Van den Berghe, G. Van Den Bosch, L. van den Brink, G.R. van der Goot, F.G. van der Klei, I.J. van der Laan, L.J.W. van Doorn, W.G. van Egmond, M. van Golen, K.L. Van Kaer, L. Campagne, M.L. Vandenabeele, P. Vandenberghe, W. Vanhorebeek, I. Varela-Nieto, I. Vasconcelos, M.H. Vasko, R. Vavvas, D.G. Vega-Naredo, I. Velasco, G. Velentzas, A.D. Velentzas, P.D. Vellai, T. Vellenga, E. Vendelbo, M.H. Venkatachalam, K. Ventura, N. Ventura, S. Veras, P.S.T. Verdier, M. Vertessy, B.G. Viale, A. Vidal, M. Vieira, H.L.A. Vierstra, R.D. Vigneswaran, N. Vij, N. Vila, M. Villar, M. Villar, V.H. Villarroya, J. Vindis, C. Viola, G. Viscomi, M.T. Vitale, G. Vogl, D.T. Voitsekhovskaja, O.V. von Haefen, C. von Schwarzenberg, K. Voth, D.E. Vouret-Craviari, V. Vuori, K. Vyas, J.M. Waeber, C. Walker, C.L. Walker, M.J. Walter, J. Wan, L. Wan, X. Wang, B. Wang, C. Wang, C.-Y. Wang, C. Wang, C. Wang, C. Wang, D. Wang, F. Wang, F. Wang, G. Wang, H.-J. Wang, H. Wang, H.-G. Wang, H. Wang, H.-D. Wang, J. Wang, J. Wang, M. Wang, M.-Q. Wang, P.-Y. Wang, P. Wang, R.C. Wang, S. Wang, T.-F. Wang, X. Wang, X.-J. Wang, X.-W. Wang, X. Wang, X. Wang, Y. Wang, Y. Wang, Y. Wang, Y.-J. Wang, Y. Wang, Y. Wang, Y.T. Wang, Y. Wang, Z.-N. Wappner, P. Ward, C. Ward, D.M.V. Warnes, G. Watada, H. Watanabe, Y. Watase, K. Weaver, T.E. Weekes, C.D. Wei, J. Weide, T. Weihl, C.C. Weindl, G. Weis, S.N. Wen, L. Wen, X. Wen, Y. Westermann, B. Weyand, C.M. White, A.R. White, E. Whitton, J.L. Whitworth, A.J. Wiels, J. Wild, F. Wildenberg, M.E. Wileman, T. Wilkinson, D.S. Wilkinson, S. Willbold, D. Williams, C. Williams, K. Williamson, P.R. Winklhofer, K.F. Witkin, S.S. Wohlgemuth, S.E. Wollert, T. Wolvetang, E.J. Wong, E. Wong, G.W. Wong, R.W. Wong, V.K.W. Woodcock, E.A. Wright, K.L. Wu, C. Wu, D. Wu, G.S. Wu, J. Wu, J. Wu, M. Wu, M. Wu, S. Wu, W.K.K. Wu, Y. Wu, Z. Xavier, C.P.R. Xavier, R.J. Xia, G.-X. Xia, T. Xia, W. Xia, Y. Xiao, H. Xiao, J. Xiao, S. Xiao, W. Xie, C.-M. Xie, Z. Xie, Z. Xilouri, M. Xiong, Y. Xu, C. Xu, C. Xu, F. Xu, H. Xu, H. Xu, J. Xu, J. Xu, J. Xu, L. Xu, X. Xu, Y. Xu, Y. Xu, Z.-X. Xu, Z. Xue, Y. Yamada, T. Yamamoto, A. Yamanaka, K. Yamashina, S. Yamashiro, S. Yan, B. Yan, B. Yan, X. Yan, Z. Yanagi, Y. Yang, D.-S. Yang, J.-M. Yang, L. Yang, M. Yang, P.-M. Yang, P. Yang, Q. Yang, W. Yang, W.Y. Yang, X. Yang, Y. Yang, Y. Yang, Z. Yang, Z. Yao, M.-C. Yao, P.J. Yao, X. Yao, Z. Yao, Z. Yasui, L.S. Ye, M. Yedvobnick, B. Yeganeh, B. Yeh, E.S. Yeyati, P.L. Yi, F. Yi, L. Yin, X.-M. Yip, C.K. Yoo, Y.-M. Yoo, Y.H. Yoon, S.-Y. Yoshida, K.-I. Yoshimori, T. Young, K.H. Yu, H. Yu, J.J. Yu, J.-T. Yu, J. Yu, L. Yu, W.H. Yu, X.-F. Yu, Z. Yuan, J. Yuan, Z.-M. Yue, B.Y.J.T. Yue, J. Yue, Z. Zacks, D.N. Zacksenhaus, E. Zaffaroni, N. Zaglia, T. Zakeri, Z. Zecchini, V. Zeng, J. Zeng, M. Zeng, Q. Zervos, A.S. Zhang, D.D. Zhang, F. Zhang, G. Zhang, G.-C. Zhang, H. Zhang, H. Zhang, H. Zhang, J. Zhang, J. Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.

Published
2016

8. Abstracts of papers presented at the 12th Conference of the Weed Science Society of Israel

Author

J. Gressel, J. Friedman, S. Chyen, D. Stern, O. Barazani, Paulina Keller, Y. Kleifeld, Miriam Zilberstein, A. Dinoor, Nava Eshed, S. Golan, Ora Edut, A. Lisaii, H. Buxbaum, R. Gadish, M. Horowitz, L. Afgin, G. Herzlinger, A. Grinstein, H. Aviram, J. Secor, Rina Varsano, A. Tal, B. Rubin, Ariela Leist, J. Caseley, M. Negbi, R. Scalla, T. Yaacoby, J. C. Hall, G. R. Stephenson, Tamas Komives, J. Gressfx, M. Sibony, Y. Benyamini, S. R. Moss, J. C. Caseley, D. Chamovitz, Iris Pecker, G. Sandmann, J. Hirschberg, A. Perl, R. Perl-Treves, S. Galili, Dvora Aviv, E. Shalgi, S. Malkin, E. Galun, M. Schonfeld, M. A. K. Jansen, A. Trebst, M. Edelman, Hadar Kless, N. Ohad, Y. Evron, M. Yogev, D. M. Joel, D. Losner-Goshen, A. M. Mayer, G. Ben-Mod, A. Bargutti, R. Jacobsohn, E. Eldar, Adiva Shomer-Ilan, Y. Goldwasser, E. Levitin, O. Arav, Dana Kahana, null Rinatrusso, D. Palevitz, A. Levy, Orly Michael, D. Baum, A. Nir, A. Raz, Z. Ben-Arie, D. Carmon, R. Epstein, J. Baum, Y. Oren, S. Glidal, S. Graph, U. Luchinsky, A. Hadar, S. Kethain, S. Glidai, M. Gootman, Y. Noy, H. Apelblat, H. Bucsbaum, Y. Weiss, M. J. Pinthus, B. Retig, W. Lerer, N. Barnea, R. Gelman, A. Daube, U. Rosenberg, and S. Ovadia

Subjects
Agriculture, business.industry, Insect Science, Ecology (disciplines), Weed science, Plant Science, Biology, Social science, business
Published
1992
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9. Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene

Author

S, Galili, D, Guenoune, S, Wininger, B, Hana, A, Schupper, B, Ben-Dor, and Y, Kapulnik

Subjects
Plant Leaves, Threonine, Escherichia coli, Gene Expression, Aspartate Kinase, Plants, Genetically Modified, Recombinant Proteins, Medicago sativa, Protein Binding
Abstract

Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins.

Published
2000

10. Expression of Soybean Vegetative Storage Proteins (VSPα) in Tobacco Leaves

Author

Shmuel Wolf, D. Guenoune, S. Galili, S. Wininger, H. Badani, Bruria Ben-Dor, and R. Amir

Subjects
chemistry.chemical_classification, Horticulture, chemistry, Transgene, fungi, Translational regulation, Botany, Wild type, food and beverages, Storage protein, Genetically modified crops, Biology
Abstract

Vegetative storage proteins (VSPs) were originally identified as leaf proteins that accumulate to about 45% of the total soluble leaf proteins in depodded soybean plants (Staswick, 1990). In this work we expressed soybean VSPα in transgenic tobacco plants under the control of CaMV 35S promoter. Analysis by SDS Polyacrylamide gels revealed a similar molecular weight for the soybean VSPα in transgenic and in wild type (WT) plants. This observation suggests that soybean VSPα in transgenic plants follows corrected processing. We infer that tobacco plants provide a suitable system for studying post-transcriptional and post translation regulation of VSP.

Published
1999
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11. Studies on MsENOD40 gene expression in alfalfa (Medicago sativa L.) and white sweetclover (Melilotus alba Desr.)

Author

V. To, Ann M. Hirsch, Y. Eshead, N. Atzmon, O. Shaul, S. Galili, Yoram Kapulnik, Smadar Wininger, P. van Rhijn, Y. Li, and Y. Fang

Subjects
chemistry.chemical_classification, fungi, food and beverages, Biology, biology.organism_classification, White (mutation), chemistry.chemical_compound, chemistry, Auxin, Gene expression, Botany, Cytokinin, heterocyclic compounds, Melilotus, Medicago sativa, Hormone
Abstract

Plant hormones have been postulated to be involved with nodule development for at least 60 years (see Hirsch and Fang, 1994 for review). One of the most enigmatic of the plant hormones is cytokinin. Little is known about its biosynthesis in the plant or its mechanism of action. Numerous investigations have shown that there is an interaction between cytokinin and auxin, but exactly how these two phytohormones mediate development, especially in the root, is unclear.

Published
1997
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13. Genetic characterization and mapping of the shell-strength trait in peanut.

Author

Israel GB, Kunta S, Mlelwa W, Harel A, Gupta K, Levy Y, Galili S, and Hovav R

Subjects
Phenotype, Arachis genetics, Arachis growth & development, Quantitative Trait Loci, Chromosome Mapping
Abstract

Background: Shell strength is an important trait in peanuts that impacts shell breakage and yield. Despite its significance, the genetic basis of shell strength in peanuts remains largely unknown, and the current methods for rating this trait are qualitative and subjective. This study aimed to investigate the genetics of shell strength using a segregating recombinant-inbred-line (RIL) population derived from the hard-shelled cultivar 'Hanoch' and the soft-shelled cultivar 'Harari'., Results: Initially, a quantitative method was developed using a texture analyzer, focusing on the proximal part of isolated shells with a P/5 punching probe. This method revealed significant differences between Hanoch and Harari. Shell strength was then measured in 235 RILs across two distinct environments, revealing a normal distribution with some RILs exhibiting shell strength values beyond those of the parental lines, indicating transgressive segregation. Analysis of variance indicated significant effects for the RILs, with no effects of block or year, and a broad-sense heritability estimate of 0.675, indicating a substantial genetic component. Using an existing genetic map, we identified three QTLs for shell strength, with one major QTL (qSSB02) explaining 18.7% of the phenotypic variation. The allelic status of qSSB02 corresponded significantly with cultivar designation for in-shell or shelled types over four decades of Israeli peanut breeding. Physical and compositional analyses revealed that Hanoch has a higher shell density than Harari, rather than any difference in shell thickness, and is associated with increased levels of lignin, cellulose, and crude fiber., Conclusions: These findings provide valuable insights into the genetic and compositional factors that influence shell strength in peanut, laying a foundation for marker-assisted selection in breeding programs focused on improving pod hardness in peanuts., (© 2024. The Author(s).)

Published
2024
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14. The potential of young vegetative quinoa (Chenopodium quinoa) as a new sustainable protein-rich winter leafy crop under Mediterranean climate.

Author

Rubinovich L, Dagan R, Lugasi Y, Galili S, and Asher A

Subjects
Humans, Animals, Climate, Seasons, Edible Grain, Israel, Chenopodium quinoa chemistry
Abstract

The demand for protein products has significantly risen in the last few years. In western countries, animals are the primary source of protein; however, plants could take a share of this market due to lower production costs, among other advantages such as a lower environmental footprint. Quinoa (Chenopodium quinoa Willd.) is a well-known but under-utilized protein-rich crop, commonly cultivated for grain production. These plants were recently evaluated for their use as a non-traditional, green leafy crop. Here we assessed the potential of young vegetative quinoa as a new sustainable winter leafy crop in Israel-serving as a model for Mediterranean semi-arid regions, by evaluating yield, protein content and quality. Five quinoa accessions were sown on three winter sowing dates over two consecutive years. Plants were harvested when they reached 10% dry matter (DM). DM yield ranged between 574 and 1,982 kg ha-1 and was generally higher in the second year. Protein content ranged from 14.4-34% and was generally higher in the first year. Protein yield ranged from 111-471 kg ha-1 and was greatest on the December sowing date. DM and protein yields were positively correlated with plant density. Protein content was negatively correlated with plant density and DM yield. Our findings show that 200 g DM of young vegetative quinoa can meet the protein and most essential amino acid requirements for a 70 kg human adult. Prospects for cultivating young vegetative quinoa in Mediterranean countries as a new sustainable, protein-rich winter leafy crop are therefore high, as supported by its high protein yields and quality, and its requirement for only scant irrigation. Further studies should examine economic and other agrotechnical parameters toward the geographical distribution and expansion of young vegetative quinoa cultivation., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2023 Rubinovich et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

Published
2023
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15. Novel Mutation in the Acetohydroxyacid Synthase (AHAS), Gene Confers Imidazolinone Resistance in Chickpea Cicer arietinum L. Plants.

Author

Galili S, Hershenhorn J, Edelman M, Sobolev V, Smirnov E, Amir-Segev O, Bellalou A, and Dor E

Abstract

Chickpea ( Cicer arietinum L.) is an important crop in crop-rotation management in Israel. Imidazolinone herbicides have a wide spectrum of weed control, but chickpea plants are sensitive to acetohydroxyacid synthase (AHAS; also known as acetolactate synthase [ALS]) inhibitors. Using the chemical mutagen ethyl methanesulfonate (EMS), we developed a chickpea line (M2033) that is resistant to imidazolinone herbicides. A point mutation was detected in one of the two genes encoding the AHAS catalytic subunit of M2033. The transition of threonine to isoleucine at position 192 (203 according to Arabidopsis ) conferred resistance of M2033 to imidazolinones, but not to other groups of AHAS inhibitors. The role of this substitution in the resistance of line M2033 was proven by genetic transformation of tobacco plants. This resistance showed a single-gene semidominant inheritance pattern. Conclusion: A novel mutation, T192I (T203I according to Arabidopsis ), providing resistance to IMI herbicides but not to other groups of AHAS inhibitors, is described in the AHAS1 protein of EMS-mutagenized chickpea line M2033.

Published
2021
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16. Characterization of a Chickpea Mutant Resistant to Phelipanche aegyptiaca Pers. and Orobanche crenata Forsk.

Author

Galili S, Hershenhorn J, Smirnov E, Yoneyama K, Xie X, Amir-Segev O, Bellalou A, and Dor E

Abstract

Chickpea ( Cicer arietinum L.) is a major pulse crop in Israel grown on about 3000 ha spread, from the Upper Galilee in the north to the North-Negev desert in the south. In the last few years, there has been a gradual increase in broomrape infestation in chickpea fields in all regions of Israel. Resistant chickpea cultivars would be simple and effective solution to control broomrape. Thus, to develop resistant cultivars we screened an ethyl methanesulfonate (EMS) mutant population of F01 variety (Kabuli type) for broomrape resistance. One of the mutant lines (CCD7M14) was found to be highly resistant to both Phelipanche aegyptiaca and Orobanche crenata. The resistance mechanism is based on the inability of the mutant to produce strigolactones (SLs)-stimulants of broomrape seed germination. LC/MS/MS analysis revealed the SLs orobanchol, orobanchyl acetate, and didehydroorobanchol in root exudates of the wild type, but no SLs could be detected in the root exudates of CCD7M14. Sequence analyses revealed a point mutation (G-to-A transition at nucleotide position 210) in the Carotenoid Cleavage Dioxygenase 7 (CCD7) gene that is responsible for the production of key enzymes in the biosynthesis of SLs. This nonsense mutation resulted in a CCD7 stop codon at position 70 of the protein. The influences of the CCD7M14 mutation on chickpea phenotype and chlorophyll, carotenoid, and anthocyanin content were characterized.

Published
2021
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17. Biofilm formation onto starch fibres by Bacillus subtilis governs its successful adaptation to chickpea milk.

Author

Rajasekharan SK, Paz-Aviram T, Galili S, Berkovich Z, Reifen R, and Shemesh M

Subjects
Bacterial Proteins genetics, Starch, Bacillus subtilis genetics, Bacillus subtilis growth & development, Biofilms, Cicer chemistry
Abstract

Beneficial biofilms may confer effective adaptation to food matrices that assist bacteria in enduring hostile environmental conditions. The matrices, for instance, dietary fibres of various food products, might serve as a natural scaffold for bacterial cells to adhere and grow as biofilms. Here, we report on a unique interaction of Bacillus subtilis cells with the resistant starch fibresof chickpea milk (CPM), herein CPM fibres, along with the production of a reddish-pink pigment. Genetic analysis identified the pigment as pulcherrimin, and also revealed the involvement of Spo0A/SinI pathway in modulating the observed phenotypes. Besides, through successful colonization of the CPM fibres, the wild-type cells of B. subtilis displayed enhanced survivability and resilience to environmental stress, such as heat and in vitro gastrointestinal treatments. In total, we infer that the biofilm formation on CPM fibres is an adaptation response of B. subtilis for strategic survival., (© 2020 The Authors. Published by John Wiley & Sons Ltd and Society for Applied Microbiology.)

Published
2021
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18. The Effects of Herbicides Targeting Aromatic and Branched Chain Amino Acid Biosynthesis Support the Presence of Functional Pathways in Broomrape.

Author

Dor E, Galili S, Smirnov E, Hacham Y, Amir R, and Hershenhorn J

Abstract

It is not clear why herbicides targeting aromatic and branched-chain amino acid biosynthesis successfully control broomrapes-obligate parasitic plants that obtain all of their nutritional requirements, including amino acids, from the host. Our objective was to reveal the mode of action of imazapic and glyphosate in controlling the broomrape Phelipanche aegyptiaca and clarify if this obligatory parasite has its own machinery for the amino acids biosynthesis. P. aegyptiaca callus was studied to exclude the indirect influence of the herbicides on the parasite through the host plant. Using HRT - tomato plants resistant to imidazolinone herbicides, it was shown that imazapic is translocated from the foliage of treated plants to broomrape attachments on its roots and controls the parasite. Both herbicides inhibited P. aegyptiaca callus growth and altered the free amino acid content. Blasting of Arabidopsis thaliana 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) and acetolactate synthase (ALS) cDNA against the genomic DNA of P. aegyptiaca yielded a single copy of each homolog in the latter, with about 78 and 75% similarity, respectively, to A. thaliana counterparts at the protein level. We also show for the first time that both EPSPS and ALS are active in P. aegyptiaca callus and flowering shoots and are inhibited by glyphosate and imazapic, respectively. Thus leading to deficiency of those amino acids in the parasite tissues and ultimately, death of the parasite, indicating the ability of P. aegyptiaca to synthesize branched-chain and aromatic amino acids through the activity of ALS and EPSPS, respectively.

Published
2017
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19. Determination of polyphenols, flavonoids, and antioxidant capacity in colored chickpea (Cicer arietinum L.).

Author

Segev A, Badani H, Kapulnik Y, Shomer I, Oren-Shamir M, and Galili S

Subjects
Food Analysis methods, Polyphenols, Antioxidants analysis, Cicer chemistry, Flavonoids analysis, Phenols analysis
Abstract

Dry legumes are staple and potentially functional food, being a good source of polyphenols, flavonoids, and antioxidant activity. The objective of this study was to determine the total polyphenol content (TPC), total flavonoid content (TFC), and their relation with antioxidant capacity in 17 chickpea lines having colored seed coats (black, red, brown, green, rubiginous, gray, yellow, cream, or beige). The seed coat usually contains more than 95% of these compounds. In this study, both TPC and TFC varied significantly among different lines and were highly correlated to antioxidant activity. Colored seeds contained up to 13-, 11-, and 31-fold more TPC, TFC, and antioxidant activity, respectively, than cream- and beige-color seeds. Thus, colored chickpea could be a potentially functional food in addition to its traditional role of providing dietary proteins and dietary fibers.

Published
2010
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20. Poor competitive fitness of transgenically mitigated tobacco in competition with the wild type in a replacement series.

Author

Al-Ahmad H, Galili S, and Gressel J

Subjects
Arabidopsis Proteins genetics, Drug Resistance genetics, Genetic Engineering, Genotype, Herbicides pharmacology, Imidazoles pharmacology, Niacin analogs & derivatives, Niacin pharmacology, Phenotype, Plant Leaves growth & development, Plants, Genetically Modified, Reproduction drug effects, Reproduction genetics, Time Factors, Nicotiana drug effects, Transgenes genetics, Selection, Genetic, Nicotiana genetics, Nicotiana physiology
Abstract

Transgenic crops can interbreed with other crop cultivars or with related weeds, increasing the potential of the hybrid progeny for competition. To prevent generating competitive hybrids, we previously tested tobacco (Nicotiana tabacum L.) as a model for validating the transgenic mitigation (TM) concept using tandem constructs where a gene of choice is linked to mitigating genes that are positive or neutral to the crop, but deleterious to a recipient under competition. Here, we examine the efficacy of the TM concept at various ratios of transgenically mitigated tobacco in competition with the wild type tobacco in an ecological replacement series. The dwarf/herbicide-resistant TM transgenic plants cultivated alone under self-competition grew well and formed many more flowers than the tall wild type, which is an indication of greater reproductivity. In contrast to the wild type, TM flowering was almost completely suppressed in mixed cultures at most TM/wild type ratios up to 75% transgenic, as the TM plants were extremely unfit to reproduce. In addition, homozygous TM progeny had an even lower competitive fitness against the wild type than hemizygous/homozygous TM segregants. Thus, the TM technology was effective in reducing the risk of transgene establishment of intraspecific transgenic hybrids at different competitive levels, at the close spacing typical of weed populations.

Published
2005
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21. Enhanced levels of methionine and cysteine in transgenic alfalfa (Medicago sativa L.) plants over-expressing the Arabidopsis cystathionine gamma-synthase gene.

Author

Avraham T, Badani H, Galili S, and Amir R

Abstract

With the aim of increasing the methionine level in alfalfa (Medicago sativa L.) and thus improving its nutritional quality, we produced transgenic alfalfa plants that expressed the Arabidopsis cystathionine gamma-synthase (AtCGS), the enzyme that controls the synthesis of the first intermediate metabolite in the methionine pathway. The AtCGS cDNA was driven by the Arabidopsis rubisco small subunit promoter to obtain expression in leaves. Thirty transgenic plants were examined for the transgene protein expression, and four lines with a high expression level were selected for further work. In these lines, the contents of methionine, S-methylmethionine (SMM), and methionine incorporated into the water-soluble protein fraction increased up to 32-fold, 19-fold, and 2.2-fold, respectively, compared with that in wild-type plants. Notably, in these four transgenic lines, the levels of free cysteine (the sulphur donor for methionine synthesis), glutathione (the cysteine storage and transport form), and protein-bound cysteine increased up to 2.6-fold, 5.5-fold, and 2.3-fold, respectively, relative to that in wild-type plants. As the transgenic alfalfa plants over-expressing AtCGS had significantly higher levels of both soluble and protein-bound methionine and cysteine, they may represent a model and target system for improving the nutritional quality of forage crops.

Published
2005
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22. Tandem constructs to mitigate transgene persistence: tobacco as a model.

Author

Al-Ahmad H, Galili S, and Gressel J

Subjects
Acetolactate Synthase genetics, Arabidopsis Proteins genetics, DNA Primers, Gene Frequency, Genetics, Population, Phenotype, Sequence Analysis, DNA, Nicotiana genetics, Genetic Engineering methods, Plants, Genetically Modified genetics, Plants, Genetically Modified growth & development, Nicotiana growth & development, Transgenes genetics
Abstract

Some transgenic crops can introgress genes into other varieties of the crop, to related weeds or themselves remain as 'volunteer' weeds, potentially enhancing the invasiveness or weediness of the resulting offspring. The presently suggested mechanisms for transgene containment allow low frequency of gene release (leakage), requiring the mitigation of continued spread. Transgenic mitigation (TM), where a desired primary gene is tandemly coupled with mitigating genes that are positive or neutral to the crop but deleterious to hybrids and their progeny, was tested as a mechanism to mitigate transgene introgression. Dwarfism, which typically increases crop yield while decreasing the ability to compete, was used as a mitigator. A construct of a dominant ahasR (acetohydroxy acid synthase) gene conferring herbicide resistance in tandem with the semidominant mitigator dwarfing Delta gai (gibberellic acid-insensitive) gene was transformed into tobacco (Nicotiana tabacum). The integration and the phenotypic stability of the tandemly linked ahasR and Delta gai genomic inserts in later generations were confirmed by polymerase chain reaction. The hemizygous semidwarf imazapyr-resistant TM T1 (= BC1) transgenic plants were weak competitors when cocultivated with wild type segregants under greenhouse conditions and without using the herbicide. The competition was most intense at close spacings typical of weed offspring. Most dwarf plants interspersed with wild type died at 1-cm, > 70% at 2.5-cm and 45% at 5-cm spacing, and the dwarf survivors formed no flowers. At 10-cm spacing, where few TM plants died, only those TM plants growing at the periphery of the large cultivation containers formed flowers, after the wild type plants terminated growth. The highest reproductive TM fitness relative to the wild type was 17%. The results demonstrate the suppression of crop-weed hybrids when competing with wild type weeds, or such crops as volunteer weeds, in seasons when the selector (herbicide) is not used. The linked unfitness would be continuously manifested in future generations, keeping the transgene at a low frequency.

Published
2004
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23. Coexpression of the soybean vegetative storage protein beta subunit (S-VSPbeta) either with the bacterial feedback-insensitive dihydrodipicolinate synthase or with S-VSPalpha stabilizes the S-VSPbeta transgene protein and enhances lysine production in transgenic tobacco plants.

Author

Guenoune D, Amir R, Badani H, Wolf S, and Galili S

Subjects
Animals, Chloroplasts metabolism, Feedback, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Humans, Hydro-Lyases genetics, Plant Leaves genetics, Plant Proteins genetics, Plants, Genetically Modified, Glycine max, Nicotiana genetics, Hydro-Lyases metabolism, Lysine biosynthesis, Plant Leaves metabolism, Plant Proteins metabolism, Nicotiana metabolism, Transgenes genetics
Abstract

Soybean vegetative storage proteins (S-VSPs) are lysine-rich leaf proteins, originally found to accumulate to high levels in depodded soybean plants. In the present study, we overexpressed S-VSPbeta, the ruminant stable subunit of the S-VSP genes, in transgenic tobacco plants. The S-VSPbeta protein accumulated in all organs studied, but its level declined drastically with leaf age. This instability of S-VSPbeta could be overcome either by elevating free lysine levels or by coexpressing S-VSPbeta with S-VSPbeta. High levels of rumen-stable, lysine-rich proteins is expected to improve absorption of lysine by ruminants. Furthermore, the expression of S-VSPs in heterologous plants led to a significant increase in total soluble lysine, suggesting that these proteins may also permit better assimilation of lysine by humans and monogastric animals.

Published
2003
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24. Combined expression of S-VSPalpha in two different organelles enhances its accumulation and total lysine production in leaves of transgenic tobacco plants.

Author

Guenoune D, Amir R, Badani H, Wolf S, and Galili S

Subjects
Acid Phosphatase metabolism, Chloroplasts metabolism, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Plant Leaves genetics, Plants, Genetically Modified, Nicotiana genetics, Vacuoles metabolism, Lysine biosynthesis, Organelles metabolism, Plant Leaves metabolism, Plant Proteins metabolism, Nicotiana metabolism
Abstract

Soybean vegetative storage proteins (S-VSPs) accumulate to high levels in vacuoles of both wild types and heterologous plants. Here it is shown that directing S-VSPalpha to two different organelles-chloroplasts and vacuoles-in a single transgenic plant significantly increased its accumulation. Accumulation of S-VSPalpha in heterologous plants correlated with total soluble lysine. Using this approach with essential amino-acid-rich transgene proteins may lead to a breakthrough in improving plant nutritional quality.

Published
2002
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25. Resistance of soybean vegetative storage proteins (S-VSPs) to proteolysis by rumen microorganisms.

Author

Guenoune D, Landau S, Amir R, Badani H, Devash L, Wolf S, and Galili S

Subjects
Animals, Blotting, Western, Cattle, Female, Gene Expression, Kinetics, Plant Leaves metabolism, Plant Proteins genetics, Plants, Genetically Modified, Recombinant Proteins metabolism, Nicotiana genetics, Nicotiana metabolism, Endopeptidases metabolism, Plant Proteins metabolism, Rumen microbiology
Abstract

Soybean vegetative storage proteins (S-VSPs) are lysine-rich and, hence, are potentially of high nutritive value for high productive ruminants. Using S-VSPs from wild-type soybean and from transgenic tobacco plants expressing either one of the two S-VSPs subunits (S-VSP alpha or S-VSP beta) or both, we tested their stability in cow rumen fluid under in situ conditions, using SDS-polyacrylamide gel electrophoresis. Proteolysis and degradation pattern of S-VSPs from transgenic tobacco leaves occurred relatively fast compared with that of wild-type (WT) soybean plants. Comparing the two S-VSPs subunits expressed in transgenic plants, we found that S-VSP alpha was degraded much faster than S-VSP beta. The degradation pattern of S-VSPs in transgenic tobacco plants expressing both subunits resembled that of WT soybean. In contrast, the degradation pattern of transgenic tobacco plants expressing a single subunit was different. These finding suggest that the quaternary structure of S-VSPs may be an important factor determining their resistance to rumen degradation. Our results also suggest that the stability to rumen proteolysis of a given protein, when expressed in a transgenic plant, may not always be predictable and has to be verified.

Published
2002
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26. The defense response elicited by the pathogen Rhizoctonia solani is suppressed by colonization of the AM-fungus Glomus intraradices.

Author

Guenoune D, Galili S, Phillips DA, Volpin H, Chet I, Okon Y, and Kapulnik Y

Abstract

Defense responses of alfalfa roots to the pathogenic fungus Rhizoctonia solani were reduced significantly in roots simultaneously infected with the vesicular arbuscular mycorrhizal (AM) fungus Glomus intraradices. R. solani induced five- to tenfold increases in the steady-state levels of chalcone isomerase and isoflavone reductase mRNAs a doubling of root peroxidase activity and a marked autofluorescence in the infected tissue. These changes were inhibited by the presence of G. intraradices. Interestingly, germination of G. intraradices spores and hyphal elongation were sensitive to low concentrations (2 µM) of medicarpin-3-O-glucoside, an isoflavonoid phytoalexin that accumulated both in roots colonized by the pathogenic fungus as well as in AM-treated roots receiving high P, where no colonization by the beneficial fungus occurred. These data support the hypothesis that during early stages of colonization by G. intraradices, suppression of defense-related properties is associated with the successful establishment of AM symbiosis.

Published
2001
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27. RFLP-based analysis of three RbcS subfamilies in diploid and polyploid species of wheat.

Author

Galili S, Avivi Y, Millet E, and Feldman M

Subjects
DNA Probes, Diploidy, Genes, Plant, Phylogeny, Polyploidy, Species Specificity, Triticum enzymology, Chromosome Mapping, Multigene Family, Polymorphism, Restriction Fragment Length, Ribulose-Bisphosphate Carboxylase genetics, Triticum classification, Triticum genetics
Abstract

The RbcS multigene family of hexaploid (bread) wheat, Triticum aestivum (genome BBAADD), which encodes the small subunit of Rubisco, comprises at least 22 genes. Based on their 3' non-coding sequences, these genes have been classified into four subfamilies (SFs), of which three (SF-2, SF-3 and SF-4) are located on chromosomes of homoeologous group 2 and one (SF-1) on homoeologous group 5. In the present study we hybridized three RbcS subfamily-specific probes (for SF-1, SF-2 and SF-3) to total DNA digested with four restriction enzymes and analyzed the RFLP patterns of these subfamilies in eight diploid species of Aegilops and Triticum, and in two tetraploid and one hexaploid species of wheat (the diploid species are the putative progenitors of the polyploid wheats). The three subfamilies varied in their level of polymorphism, with SF-2 being the most polymorphic in all species. In the diploids, the order of polymorphism was SF-2 > SF-3 > SF-1, and in the polyploids SF-2 > SF-1 > SF-3. The RbcS genes of the conserved SF-1 were previously reported to have the highest expression levels in all the wheat tissues studied, indicating a negative correlation between polymorphism and gene expression. Among the diploids, the species with the D and the S genomes were the most polymorphic and the A-genome species were the least polymorphic. The polyploids were less polymorphic than the diploids. Within the polyploids, the A genome was somewhat more polymorphic than the B genome, while the D genome was the most conserved. Among the diploid species with the A genome, the RFLP pattern of T. urartu was closer to that of the A genome of the common wheat cultivar Chinese Spring (CS) than to that of T. monococcum. The pattern in Ae. tauschii was similar to that of the D genome of CS. Only partial resemblance was found between the RFLP patterns of the species with the S genome and the B genome of CS.

Published
2000
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28. Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene.

Author

Galili S, Guenoune D, Wininger S, Hana B, Schupper A, Ben-Dor B, and Kapulnik Y

Subjects
Aspartate Kinase metabolism, Escherichia coli enzymology, Escherichia coli genetics, Gene Expression, Medicago sativa metabolism, Plant Leaves metabolism, Plants, Genetically Modified metabolism, Protein Binding, Recombinant Proteins metabolism, Aspartate Kinase genetics, Medicago sativa genetics, Threonine biosynthesis
Abstract

Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins.

Published
2000
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29. Mycorrhiza-induced changes in disease severity and PR protein expression in tobacco leaves

Author

Shaul O, Galili S, Volpin H, Ginzberg I I, Elad Y, Chet I I, and Kapulnik Y

Abstract

The development of leaf disease symptoms and the accumulation of pathogenesis-related (PR) proteins were monitored in leaves of tobacco (Nicotiana tabacum cv. Xanthinc) plants colonized by the arbuscular mycorrhizal fungus Glomus intraradices. Leaves of mycorrhizal plants infected with the leaf pathogens Botrytis cinerea or tobacco mosaic virus showed a higher incidence and severity of necrotic lesions than those of nonmycorrhizal controls. Similar plant responses were obtained at both low (0.1 mM) and high (1.0 mM) nutritional P levels and with mutant plants (NahG) that are unable to accumulate salicylic acid. Application of PR-protein activators induced PR-1 and PR-3 expression in leaves of both nonmycorrhizal and mycorrhizal plants; however, accumulation and mRNA steady-site levels of these proteins were lower, and their appearance delayed, in leaves of the mycorrhizal plants. Application of 0.3 mM phosphate to the plants did not mimic the delay in PR expression observed in the mycorrhizal tobacco. Together, these data strongly support the existence of regulatory processes, initiated in the roots of mycorrhizal plants, that modify disease-symptom development and gene expression in their leaves.

Published
1999
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30. Expression of early nodulin genes in alfalfa mycorrhizae indicates that signal transduction pathways used in forming arbuscular mycorrhizae and Rhizobium-induced nodules may be conserved.

Author

van Rhijn P, Fang Y, Galili S, Shaul O, Atzmon N, Wininger S, Eshed Y, Lum M, Li Y, To V, Fujishige N, Kapulnik Y, and Hirsch AM

Abstract

Transcripts for two genes expressed early in alfalfa nodule development (MsENOD40 and MsENOD2) are found in mycorrhizal roots, but not in noncolonized roots or in roots infected with the fungal pathogen Rhizoctonia solani. These same two early nodulin genes are expressed in uninoculated roots upon application of the cytokinin 6-benzylaminopurine. Correlated with the expression of the two early nodulin genes, we found that mycorrhizal roots contain higher levels of trans-zeatin riboside than nonmycorrhizal roots. These data suggest that there may be conservation of signal transduction pathways between the two symbioses-nitrogen-fixing nodules and phosphate-acquiring mycorrhizae.

Published
1997
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31. Production of transgenic plants containing elevated levels of lysine and threonine.

Author

Galili G, Karchi H, Shaul O, Perl A, Cahana A, Tzchori IB, Zhu XZ, and Galili S

Subjects
Aspartate Kinase biosynthesis, Biotechnology methods, Escherichia coli enzymology, Escherichia coli genetics, Gene Expression, Hydro-Lyases biosynthesis, Kinetics, Plant Leaves, Plant Proteins biosynthesis, Recombinant Proteins metabolism, Aspartate Kinase metabolism, Hydro-Lyases metabolism, Lysine metabolism, Plants, Genetically Modified metabolism, Threonine metabolism
Published
1994
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32. Enhanced oxidative-stress defense in transgenic potato expressing tomato Cu,Zn superoxide dismutases.

Author

Perl A, Perl-Treves R, Galili S, Aviv D, Shalgi E, Malkin S, and Galun E

Abstract

The two cDNAs coding for the cytosolic (cyt) and the chloroplast-located (chl) Cu,Zn superoxide dismutases (SODs) of tomato (Perl-Treves et al. 1988) were cloned into respective binary vectors and mobilized into Agrobacterium strains. Potato tuber discs were infected with either of the two agrobacterial strains and cultured on selective medium containing kanaymcin. The integration of either of the cyt or the chl SOD transgenes was verified by Southern-blot hybridization. The enzymatic activity of the additional tomato chl Cu,Zn SOD could be distinguished from endogenous SOD activity since the latter isozyme migrated faster on SOD-activity gels. Several transgenic potato lines harboring either the cyt or the chl SOD genes of tomato showed elevated tolerance to the superoxide-generating herbicide paraquat (methyl viologen). After exposure of shoots to paraquat, tolerance was recorded either by scoring symptoms visually or by measurements of photosynthesis using the photoacoustic method. Root cultures from transgenic lines that harbored the additional cyt Cu,Zn SOD gene of tomato were tolerant to methyl viologen up to 10(-5) M; a lower tolerance was recorded in roots of transgenic lines that expressed the additional chl Cu,Zn SOD of tomato.

Published
1993
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33. Identification and chromosomal location of four subfamilies of the rubisco small subunit genes in common wheat.

Author

Galili S, Galili G, Avivi Y, and Feldman M

Abstract

Three different 3' noncoding sequences of wheat rubisco small subunit (SSU) genes (RbcS) were used as probes to identify the gene members of different RbcS subfamilies in the common wheat cultivar Chinese Spring (CS). All genes of the wheat RbcS multigene family were previously assigned to the long arm of homoeologous group 5 and to the short arm of homoeologous group 2 chromosomes of cv CS. Extracted DNA from various aneuploids of these homoeologous groups was digested with four restriction enzymes and hybridized with three different 3' noncoding sequences of wheat SSU clones. All RbcS genes located on the long arm of homoeologous group 5 chromosomes were found to comprise a single subfamily, while those located on the short arm of group 2 comprised three subfamilies. Each of the ancestral diploid genomes A, B, and D has at least one representative gene in each subfamily, suggesting that the divergence into subfamilies preceded the differentiation into species. This divergence of the RbcS genes, which is presumably accompanied by a similar divergence in the 5' region, may lead to differential expression of various subfamilies in different tissues and in different developmental stages, in response to different environmental conditions. Moreover, members of one subfamily that belong to different genomes may have diverged also in the coding sequence and, consequently, code for distinguishable SSU. It is assumed that such utilization of the RbcS multigene family increases the adaptability and phenotypic plasticity of common wheat over its diploid progenitors.

Published
1992
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34. Chromosomal location of genes for Rubisco small subunit and Rubisco-binding protein in common wheat.

Author

Galili S, Galili G, and Feldman M

Abstract

The genes coding for the Rubisco small subunit (SSU) and for the α-subunit of the Rubisco-binding protein were located to chromosome arms of common wheat. HindIII-digested total DNA from the hexaploid cultivar Chinese Spring and from ditelosomic and nullisomic-tetrasomic lines was probed with these two genes, whose chromosomal location was deduced from the disappearance of or from changes in the relative intensity of the relevant band(s). The Rubisco SSU pattern consisted of 14 bands, containing at least 21 different types of DNA fragments, which were allocated to two homoeologous groups: 15 to the short arm of group 2 chromosomes (4 to 2AS, 7 to 2BS, and 4 to 2DS) and 6 to the long arm of group 5 chromosomes (2 on each of arms 5AL, 5BL, and 5DL). The pattern of the Rubisco-binding protein consisted of three bands, each containing one type of fragment. These fragments were located to be on the short arm of group 2 chromosomes. The restriction fragment length polymorphism (RFLP) patterns of several hexaploid and tetraploid lines were highly conserved, whereas the patterns of several of their diploid progenitors were more variable. The variations found in the polyploid species were mainly confined to the B genome. The patterns of the diploids T. monococcum var. urartu and Ae. squarrosa were similar to those of the A and D genome, respectively, in polyploid wheats. The pattern of T. monococcum var. boeoticum was different from the patterns of the A genome, and the patterns of the diploids Ae. speltoides, Ae. longissima, and Ae. Searsii differed from that of the B genome.

Published
1991
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35. Ribosomal protein S12 as a site for streptomycin resistance in Nicotiana chloroplasts.

Author

Galili S, Fromm H, Aviv D, Edelman M, and Galun E

Subjects
Base Sequence, Cloning, Molecular, Codon, Drug Resistance genetics, Exons, Mutation, Proline genetics, Serine genetics, Nicotiana drug effects, Chloroplasts drug effects, Plant Proteins genetics, Plants, Toxic, Ribosomal Proteins genetics, Streptomycin pharmacology, Nicotiana genetics
Abstract

A streptomycin resistant Nicotiana plastome mutant, X/strR6, was subjected to molecular analysis. In this mutant, a single nucleotide transition, C----T, in the chloroplast gene for ribosomal protein S12 alters codon 90 from proline to serine while the nucleotide sequence of the chloroplast 16 S rRNA gene is identical to that of the wild type. Mutant X/strR6 thus differs from several previously reported streptomycin resistant chloroplast mutants which are altered in the gene for 16 S rRNA.

Published
1989
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