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2. List of Contributors

Author

E.A. Abayomi, A. AghaKouchak, M. Ahmed, A.S. Akanda, V.P. Aneja, I. Annesi Maesano, S.R. Archer, J.S. Ayivor, A.K.M. Azad Hossain, D. Baldocchi, L.T. Barnard, A.P. Barros, R.J. Barthelmie, P. Bates, B.M. Beamon, D. Becker, R. Becker, A. Beckingham, H. Belhouchette, K.M. Best, B.T. Bestelmeyer, E. Betman, T. Blenckner, G. Blöschl, C. Boisvenue, S. Bolton, M. Borga, F. Booker, L.S. Borma, B. Bornstein, M.L. Brooks, J. Brown, R. Buckley, S.J. Burian, L. Burkle, C.D. Butler, M.F. Cardoso, L. Cecchi, F.S. Chapin, J. Chen, N. Chhetri, K. Chouinard, D. Christie, T. Chuluun, A.B. Cinderich, N.-E. Clausen, H. Cloke, J.E. Compton, A.C. Comrie, M. Convertino, I.M. Côté, T. Cull, D. Darko, E.S. Darling, M.A. Davis, S.D. Ddumba, M. De Felice, A.M. Degu, R. Dennis, J.H. Diaz, D. Doubler, G. D’Amato, G. Eilerts, R.W. Elmore, N. Emery, C.M. Fang, B.M. Fekete, L.P. Fong, C. Funk, H.E. Gall, K.A. Galvin, X. Gao, A.S. Gebregiorgis, A.T. Ghebreegziabhe, G. Giebel, H.R. Gimblett, J.H. Goldstein, J. Gonzalez Cruz, C. Gordon, P.Y. Groisman, S. Hajat, E. Hanna, L. Hanna, M. Hashizume, K.M. Havstad, Y. He, Z. He, B. Hill, M.T. Hoffman, T. Holcombe, F. Hossain, J.T. Hoverman, K. Hsu, G. Husak, S. Islam, S. Jha, P.T.J. Johnson, A.K. Joshi, S. Jules-Plag, A.S. Jutla, M. Kafatos, A.J. Kalyanapu, E.M. Karlsson, C. Katsman, G.A. Kiker, S.-H. Kim, W. Kimmerer, T.G.F. Kittel, T. Kjellstrom, A. Klein Tank, R.W. Knight, S. Koranteng, S. Kovats, C. Kremen, R. Lal, R.B. Lammers, M.A. Lange, S.G. Larsen, J.J. Lawler, B. Lemke, M.C. Lemos, G. Lenderink, D.J. LePoire, C. Le Quesne, I. Linkov, Z. Liu, L.H. Logan, L. López-Hoffman, C. Lowe, B.H. Luckman, S.M. Mahbubur Rahman, A.S. Mahiny, D. Manful, A.S. Mase, M.H. Masiokas, S. Mauget, A.M. Mensah, S. Mihaltcheva, A. Milewski, C.A. Miller, V. Mishra, C. Mitra, P. Modak, S.A. Moges, U.C. Mohanty, Y. Molina, S.L. Molloy, H.C. Monger, E. Montaña, A. Montanari, R. Munoz-Carpena, F. Nardi, S. Niiranen, J. Nikolic, B. Nishat, J. Niu, D. Niyogi, C.A. Nobre, D. Nukpezah, B.D. Ofori, D.S. Ojima, G.S. Okin, J.D. Olden, F.O. Otieno, P. Owens, O. Pabi, A. Papalexopoulos, F. Pappenberger, J. Park, B. Parkes, S.H. Paull, T. Pearce, D. Penna, null Perdinan, R. Perry-Hill, D.P.C. Peters, R. Picon, J. Pillich, P. Pinson, H.-P. Plag, A.M. Pollyea, W. Powers, L.S. Prokopy, S.C. Pryor, A. Rango, M. Rao, P.S.C. Rao, H. Rashid, Y.A. Rawade, D.K. Ray, A.L. Renaud, M. Rodell, A.A. Rosenberg, J. Rowland, J. Rudek, S.W. Running, P.M. Ruti, D.J. Sailor, O.E. Sala, Z. Samaras, N. Sarafoglou, O.J. Schmitz, R.J. Scholes, D. Scott, T.R. Seastedt, P. Sequera, S.M. Shah-Newaz, A. Shakeela, J.M. Shepherd, A.I. Shiklomanov, S.S. Shinde, C.K. Shum, A.H.M. Siddique-E-Akbor, K. Smart, B. Smit, M.D. Smith, E.J. Soper, S. Sorooshian, I. Souissi, B. Spencer, G. Sreckovic, R. Steiger, T.J. Stohlgren, N. Sturchio, K.N. Suding, M. Sultan, L. Sun, D.K. Swain, D.R. Taub, A. te Linde, N. Temani, L. Thompson, S.W. Todd, A. Troccolli, A.G. Tsikalakis, M.R. Tuinstra, C.E. Tweedie, E. Tweneboah-Lawson, J.M. Tylianakis, V. Vaddella, B. van den Hurk, V. Venugopal, J. Verdin, A. Viglione, R. Villalba, K. Vincent, E.R. Vivoni, J.G. Voss, I. Vouitsis, Z.N. Vrontisi, J. Wahr, T. Walsh, X. Wang, M.J. Weaver, F. Wetterhall, J.A. Winkler, A.T. Woldemichael, A.W. Wood, E. Yan, W. Yigzaw, D. Yirenya-Tawiah, D.R. Young, A.M. Zaman, C. Zavalloni, W. Zhang, and O.G. Zolina

Published
2013
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4. Escherichia coli RecX inhibits RecA recombinase and coprotease activities in vitro and in vivo

Author

H. Steven Seifert, Elizabeth A. Stohl, Joel P. Brockman, Kristin L. Burkle, Stephen C. Kowalczykowski, and Katsumi Morimatsu

Subjects
Time Factors, DNA repair, DNA damage, Ultraviolet Rays, Blotting, Western, Repressor, DNA-Directed DNA Polymerase, Biology, In Vitro Techniques, medicine.disease_cause, Biochemistry, Transduction (genetics), Adenosine Triphosphate, Bacterial Proteins, Two-Hybrid System Techniques, Recombinase, medicine, Escherichia coli, Molecular Biology, Recombination, Genetic, Escherichia coli Proteins, Hydrolysis, Serine Endopeptidases, Dose-Response Relationship, Radiation, Cell Biology, DNA, biochemical phenomena, metabolism, and nutrition, Molecular biology, Up-Regulation, Rec A Recombinases, bacteria, Repressor lexA, Homologous recombination, DNA Damage, Plasmids, Protein Binding
Abstract

In Escherichia coli the RecA protein plays a pivotal role in homologous recombination, DNA repair, and SOS repair and mutagenesis. A gene designated recX (or oraA) is present directly downstream of recA in E. coli; however, the function of RecX is unknown. In this work we demonstrated interaction of RecX and RecA in a yeast two-hybrid assay. In vitro, substoichiometric amounts of RecX strongly inhibited both RecA-mediated DNA strand exchange and RecA ATPase activity. In vivo, we showed that recX is under control of the LexA repressor and is up-regulated in response to DNA damage. A loss-of-function mutation in recX resulted in decreased resistance to UV irradiation; however, overexpression of RecX in trans resulted in a greater decrease in UV resistance. Overexpression of RecX inhibited induction of two din (damage-inducible) genes and cleavage of the UmuD and LexA repressor proteins; however, recX inactivation had no effect on any of these processes. Cells overexpressing RecX showed decreased levels of P1 transduction, whereas recX mutation had no effect on P1 transduction frequency. Our combined in vitro and in vivo data indicate that RecX can inhibit both RecA recombinase and coprotease activities.

Published
2002

5. List of Contributors

Author

M. Ian BAKER, S.V. BANDARA, L. BURKLE, Henri-Jean DROUHIN, F. FUCHS, S.D. GUNAPALA, M. HENINI, Chris van HOOF, J.E. JENSEN, J. JIANG, Masafumi KIMATA, Randolph E. LONGSHORE, Terry de LYON, H. MOHSENI, Piet De MOOR, Hartmut PRESTING, R.D. RAJAVEL, Manijeh RAZEGHI, Antoni ROGALSKI, and J.A. ROTH

Published
2002
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6. Inadvertent hypothermia

Author

N L, Burkle

Subjects
Postoperative Care, Intraoperative Care, Humans, Hypothermia, Operating Room Nursing, Intraoperative Complications, Gerontology, General Nursing, Aged, Body Temperature Regulation
Abstract

Inadvertent hypothermia can be a common, yet underestimated, hazard of the elderly surgical patient.

Published
1988

8. Nectar sugar limits larval growth of solitary bees (Hymenoptera: Megachilidae).

Author

Burkle L and Irwin R

Subjects
Animals, Bees metabolism, Larva growth & development, Larva metabolism, Reproduction, Bees growth & development, Carbohydrate Metabolism
Abstract

The bottom-up effects of plant food quality and quantity can affect the growth, survival, and reproduction of herbivores. The larvae of solitary bee pollinators, consumers of nectar and pollen, are also herbivores. Although pollen quantity and quality are known to be important for larval growth, little is known about how nectar quality limits solitary bee performance. By adding different levels of nectar sugar directly to solitary bee provisions in the subalpine of Colorado, we tested the degree to which larval performance (development time, mass, and survival) was limited by nectar sugar. We found that larval growth increased with nectar sugar addition, with the highest larval mass in the high nectar-sugar addition treatment (50% honey solution). The shortest larval development time was observed in the low nectar-sugar addition treatment (25% honey solution). Neither low nor high nectar-sugar addition affected larval survival. This study suggests that, in addition to pollen, nectar-sugar concentration can limit solitary bee larval growth and development, and nectar should be considered more explicitly as a currency governing foraging decisions related to producing optimally sized offspring. The availability and sugar content of nectar may scale up to affect bee fitness, population dynamics, and plant-pollinator mutualisms.

Published
2009
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9. The H+-sucrose cotransporter NtSUT1 is essential for sugar export from tobacco leaves

Author

Burkle L, Hibberd JM, Quick WP, Kuhn C, Hirner B, and Frommer WB

Abstract

In many species translocation of sucrose from the mesophyll to the phloem is carrier mediated. A sucrose/H+-symporter cDNA, NtSUT1, was isolated from tobacco (Nicotiana tabacum) and shown to be highly expressed in mature leaves and at low levels in other tissues, including floral organs. To study the in vivo function of NtSUT1, tobacco plants were transformed with a SUT1 antisense construct under control of the cauliflower mosaic virus 35S promoter. Upon maturation, leaves of transformants expressing reduced amounts of SUT1 mRNA curled downward, and strongly affected plants developed chloroses and necroses that led to death. The leaves exhibited impaired ability to export recently fixed 14CO2 and were unable to export transient starch during extended periods of darkness. As a consequence, soluble carbohydrates accumulated and photosynthesis was reduced. Autoradiographs of leaves show a heterogenous pattern of CO2 fixation even after a 24-h chase. The 14C pattern does not change with time, suggesting that movement of photosynthate between mesophyll cells may also be impaired. The affected lines show a reduction in the development of the root system and delayed or impaired flowering. Taken together, the effects observed in a seed plant (tobacco) demonstrate the importance of SUT1 for sucrose loading into the phloem via an apoplastic route and possibly for intermesophyll transport as well.

Published
1998
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