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7 results on '"Avni, Adi"'

1. Multi-Knock-a multi-targeted genome-scale CRISPR toolbox to overcome functional redundancy in plants.

Author

Hu Y, Patra P, Pisanty O, Shafir A, Belew ZM, Binenbaum J, Ben Yaakov S, Shi B, Charrier L, Hyams G, Zhang Y, Trabulsky M, Caldararu O, Weiss D, Crocoll C, Avni A, Vernoux T, Geisler M, Nour-Eldin HH, Mayrose I, and Shani E

Subjects
Plant Breeding, Plants genetics, Genome, Plant, CRISPR-Cas Systems, Plants, Genetically Modified genetics, Gene Editing, Clustered Regularly Interspaced Short Palindromic Repeats genetics, Arabidopsis genetics
Abstract

Plant genomes are characterized by large and complex gene families that often result in similar and partially overlapping functions. This genetic redundancy severely hampers current efforts to uncover novel phenotypes, delaying basic genetic research and breeding programmes. Here we describe the development and validation of Multi-Knock, a genome-scale clustered regularly interspaced short palindromic repeat toolbox that overcomes functional redundancy in Arabidopsis by simultaneously targeting multiple gene-family members, thus identifying genetically hidden components. We computationally designed 59,129 optimal single-guide RNAs that each target two to ten genes within a family at once. Furthermore, partitioning the library into ten sublibraries directed towards a different functional group allows flexible and targeted genetic screens. From the 5,635 single-guide RNAs targeting the plant transportome, we generated over 3,500 independent Arabidopsis lines that allowed us to identify and characterize the first known cytokinin tonoplast-localized transporters in plants. With the ability to overcome functional redundancy in plants at the genome-scale level, the developed strategy can be readily deployed by scientists and breeders for basic research and to expedite breeding efforts., (© 2023. The Author(s), under exclusive licence to Springer Nature Limited.)

Published
2023
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2. Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance.

Author

Cohen-Peer R, Schuster S, Meiri D, Breiman A, and Avni A

Subjects
Arabidopsis Proteins chemistry, Base Sequence, DNA Primers genetics, DNA, Plant genetics, DNA-Binding Proteins chemistry, DNA-Binding Proteins genetics, Gene Expression Regulation, Plant, Gene Knockout Techniques, Genes, Plant, Heat Shock Transcription Factors, Heat-Shock Proteins chemistry, Heat-Shock Proteins genetics, Heat-Shock Response genetics, Hot Temperature, Lysine chemistry, Mutagenesis, Site-Directed, Phenotype, Plant Proteins chemistry, Plant Proteins genetics, Plants, Genetically Modified, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Seedlings genetics, Seedlings metabolism, Transcription Factors chemistry, Transcription Factors genetics, Two-Hybrid System Techniques, Arabidopsis genetics, Arabidopsis metabolism, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism, DNA-Binding Proteins metabolism, Heat-Shock Proteins metabolism, Plant Proteins metabolism, Transcription Factors metabolism
Abstract

Post-translational modification of target proteins by the small ubiquitin-like modifier protein (SUMO) regulate many cellular processes. In this work we show SUMOylation of the heat shock transcription factor, AtHsfA2, in connection with the plant's response to heat stress and acquired thermotolerance. Using the Yeast two hybrid and the bimolecular fluorescence complementation system, we have found that AtSUMO1 physically interacts with AtHsfA2. Further investigation allowed us to determine that Lys 315 of AtHsfA2 is the main SUMOylation site. Overexpression of AtSUMO1 led to a decrease in AtHsfA2 transcriptional activation of heat shock promoters. We have examined the effect of AtSUMO1 on AtHsfA2 during heat shock treatments. The phenotype of seedlings overexpressing AtSUMO1 resembled the phenotype of AtHsfA2 knock out seedlings, which were more sensitive than wild type seedlings to repeated heat treatment. Furthermore, AtSUMO1 overexpressing seedlings exhibited lower expression levels of small heat shock proteins as compared with wild type seedlings after heat treatment. Based on our findings, we suggest that AtSUMO1 is involved in the regulation of AtHsfA2 in acquired thermotolerance.

Published
2010
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3. Involvement of Arabidopsis ROF2 (FKBP65) in thermotolerance.

Author

Meiri D, Tazat K, Cohen-Peer R, Farchi-Pisanty O, Aviezer-Hagai K, Avni A, and Breiman A

Subjects
Arabidopsis genetics, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism, Blotting, Western, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, DNA-Binding Proteins physiology, Electrophoresis, Polyacrylamide Gel, Fluorometry, Gene Expression Regulation, Plant genetics, Heat Shock Transcription Factors, Heat-Shock Proteins genetics, Heat-Shock Proteins metabolism, Heat-Shock Proteins physiology, Hot Temperature, Plant Proteins genetics, Plant Proteins metabolism, Plant Proteins physiology, Reverse Transcriptase Polymerase Chain Reaction, Tacrolimus Binding Proteins genetics, Tacrolimus Binding Proteins metabolism, Tacrolimus Binding Proteins physiology, Transcription Factors genetics, Transcription Factors metabolism, Transcription Factors physiology, Two-Hybrid System Techniques, Arabidopsis physiology, Arabidopsis Proteins physiology, Gene Expression Regulation, Plant physiology
Abstract

The ROF2 (FKBP65) is a heat stress protein which belongs to the FK506 Binding Protein (FKBP) family. It is homologous to ROF1 (FKBP62) which was recently shown to be involved in long term acquired thermotolerance by its interaction with HSP90.1 and modulation of the heat shock transcription factor HsfA2. In this study, we have demonstrated that ROF2 participates in long term acquired thermolerance, its mode of action being different from ROF1. In the absence of ROF2, the small heat shock proteins were highly expressed and the plants were resistant to heat stress, opposite to the effect observed in the absence of ROF1. It was further demonstrated that ROF2 transcription is modulated by HsfA2 which is also essential for keeping high levels of ROF2 during recovery from heat stress. ROF2 localization to the nucleus was observed several hours after heat stress exposure and its translocation to the nucleus was independent from the presence of HSP90.1 or HsfA2. ROF2 has been shown to interact with ROF1, to form heterodimers and it is suggested that via this interaction it can join the complex ROF1-HSP90.1- HsfA2. Transient expression of ROF2 together with ROF1 repressed transcription of small HSPs. A model describing the mode of action of ROF2 as a heat stress modulator which functions in negative feedback regulation of HsfA2 is proposed.

Published
2010
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4. The coiled-coil domain of EHD2 mediates inhibition of LeEix2 endocytosis and signaling.

Author

Bar M, Sharfman M, Schuster S, and Avni A

Subjects
Actins metabolism, Amino Acid Motifs, Arabidopsis Proteins physiology, Calcium-Binding Proteins physiology, Cytosol metabolism, Endocytosis, Exocytosis, Microscopy, Fluorescence methods, Models, Biological, Mutation, Plant Proteins metabolism, Protein Binding, Protein Structure, Tertiary, Arabidopsis metabolism, Arabidopsis Proteins chemistry, Calcium-Binding Proteins chemistry, Plant Leaves metabolism, Plant Proteins chemistry, Signal Transduction
Abstract

Endocytosis has been suggested to be crucial for the induction of plant immunity in several cases. We have previously shown that two Arabidopsis proteins, AtEHD1 and AtEHD2, are involved in endocytosis in plant systems. AtEHD2 has an inhibitory effect on endocytosis of transferrin, FM-4-64, and LeEix2. There are many works in mammalian systems detailing the importance of the various domains in EHDs but, to date, the domains of plant EHD2 that are required for its inhibitory activity on endocytosis remained unknown. In this work we demonstrate that the coiled-coil domain of EHD2 is crucial for the ability of EHD2 to inhibit endocytosis in plants, as mutant EHD2 forms lacking the coiled-coil lost the ability to inhibit endocytosis and signaling of LeEix2. The coiled-coil was also required for binding of EHD2 to the LeEix2 receptor. It is therefore probable that binding of EHD2 to the LeEix2 receptor is required for inhibition of LeEix2 internalization. We also show herein that the P-loop of EHD2 is important for EHD2 to function properly. The EH domain of AtEHD2 does not appear to be involved in inhibition of endocytosis. Moreover, AtEHD2 influences actin organization and may exert its inhibitory effect on endocytosis through actin re-distribution. The coiled-coil domain of EHD2 functions in inhibition of endocytosis, while the EH domain does not appear to be involved in inhibition of endocytosis.

Published
2009
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5. AtEHDs, novel Arabidopsis EH-domain-containing proteins involved in endocytosis.

Author

Bar M, Aharon M, Benjamin S, Rotblat B, Horowitz M, and Avni A

Subjects
Amino Acid Sequence, Animals, Arabidopsis metabolism, Arabidopsis Proteins isolation & purification, Arabidopsis Proteins metabolism, COS Cells, Calcium-Binding Proteins isolation & purification, Calcium-Binding Proteins metabolism, Chlorocebus aethiops, Cloning, Molecular, Gene Expression, Genetic Vectors, Microscopy, Confocal, Molecular Sequence Data, Phenotype, Plant Leaves genetics, Plant Leaves metabolism, Plants, Genetically Modified genetics, Plants, Genetically Modified metabolism, Protein Interaction Domains and Motifs, RNA, Plant genetics, Sequence Alignment, Sequence Homology, Amino Acid, Nicotiana genetics, Nicotiana metabolism, Transformation, Genetic, Arabidopsis genetics, Arabidopsis Proteins genetics, Calcium-Binding Proteins genetics, Endocytosis genetics
Abstract

Summary: Endocytosis is an essential process by which the eukaryotic cell internalizes exogenous material. Studies in yeast and mammalian cells have revealed that endocytosis is a complex molecular process depending on regulated interactions between a variety of proteins and lipids through specific modules. One such module is the Eps15 homology (EH) domain, a conserved modular protein-interaction domain found in several endocytic proteins. The EH-domain-containing proteins function as regulators of endocytosis through their ability to interact with other proteins involved in this process. Here we describe the isolation and characterization of two Arabidopsis EH-domain-containing proteins (AtEHD1 and AtEHD2). We show that the two proteins are involved in endocytosis in plant systems and demonstrate that the Arabidopsis EHD proteins function similarly to mammalian EHDs. Similarly to hEHD2, over-expression of AtEHD2 has an inhibitory effect on endocytosis. While transgenic plants over-expressing AtEHD1 had no detectable phenotype, downregulation of AtEHD1 caused retardation of entry of endocytosed material into plant cells.

Published
2008
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6. GCN5 modulates salicylic acid homeostasis by regulating H3K14ac levels at the 5′ and 3′ ends of its target genes

Author

Ruggieri, Valentino, Alexiou, Konstantinos, Morata, Jordi, Argyris, Jason, Pujol, Marta, Yano, Ryoichi, Nonaka, Satoko, Ezura, Hiroshi, Cigliano, Riccardo Aiese, Sanseverino, Walter, Puigdomenech, Pere, Casacuberta, Josep, Kirienko, Anna, Porozov, Yuri, Malkov, Nikita, Akhtemova, Gulnara, Le Signor, Christine, Thompson, Richard, Saffray, Christine, Dalmais, Marion, Tikhonovich, Igor, Dolgikh, Elena, Boucheham, Anouar, Sommard, Vivien, Zehraoui, Farida, Batouche, Mohamed, Israeli, David, Tahi, Fariza, Jacob, Pierre, Avni, Adi, Ligerot, Yasmine, De Saint Germain, Alexandre, Waldie, Tanya, Kadakia, Nikita, Pillot, Jean-Paul, Prigge, Michael, Aubert, Gregoire, Leyser, Ottoline, Estelle, Mark, Debellé, Frederic, Rameau, Catherine, GOUZY, Jerome, Badouin, Hélène, Lemainque, Arnaud, Vergne, Philippe, Moja, Sandrine, Choisne, Nathalie, Pont, Caroline, Carrere, Sebastien, Caissard, Jean-Claude, Couloux, Arnaud, Cottret, Ludovic, Aury, Jean-Marc, Szécsi, Judit, Madoui, Mohammed-Amin, Yang, Shu-Hua, Piola, Florence, Larrieu, Antoine, Perez, Magali, Labadie, Karine, Perrier, Lauriane, govetto, Benjamin, LABROUSSE, Yoan, Villand, Priscilla, Bardoux, Claudia, Boltz, Véronique, Lopez-Roques, Celine, Heitzler, Pascal, Vernoux, Teva, Quesneville, Hadi, Boualem, Adnane, Liu, Chang, Le Bris, Manuel, Salse, Jerome, Baudino, Sylvie, Wincker, Patrick, François, Léa, Verdenaud, Marion, Fu, Xiaopeng, Ruleman, Darcy, Dubois, Annick, Vandenbussche, Michiel, Raymond, Olivier, Just, Jérémy, Bendahmane, Mohammed, Giner, Ana, Pascual, Laura, Bourgeois, Michael, Gyetvai, Gabor, Rios, Pablo, Picó, Belén, Troadec, Christelle, Bendahmane, Abdel, Garcia-Mas, Jordi, MARTIN-HERNANDEZ, Ana Montserrat, Kim, Soonkap, Piquerez, Sophie, Ramirez-Prado, Juan, Mastorakis, Emmanouil, Veluchamy, Alaguraj, Latrasse, David, Manza-Mianza, Deborah, Brik-Chaouche, Rim, Huang, Ying, Rodriguez-Granados, Natalia, Concia, Lorenzo, Blein, Thomas, Citerne, Sylvie, Bendahmane, Abdelhafid, Bergounioux, Catherine, Crespi, Martin, Mahfouz, Magdy, Raynaud, Cécile, Hirt, Heribert, Ntoukakis, Vardis, BENHAMED, Moussa, Centre for Research in Agricultural Genomics (CRAG), IRTA, Center for Research in Agricultural Genomics, University of Tsukuba, Sequentia Biotech SL, LAboratoire PLasma et Conversion d'Energie (LAPLACE), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées, Agroécologie [Dijon], Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Université Bourgogne Franche-Comté [COMUE] (UBFC)-Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), All-Russia Research Institute for Agricultural Microbiology, University Salah Boubnider Constantine 3, Laboratoire d'Informatique de Paris-Nord (LIPN), Université Sorbonne Paris Cité (USPC)-Institut Galilée-Université Paris 13 (UP13)-Centre National de la Recherche Scientifique (CNRS), LIRE laboratory, Constantine, University of Constantine, GENETHON 3, Université Paris Saclay (COmUE), Tel Aviv University [Tel Aviv], Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Sainsbury Laboratory, University of Cambridge [UK] (CAM), University of California [San Diego] (UC San Diego), University of California, Laboratoire de chimie organique et organométallique (LCOO), Université Sciences et Technologies - Bordeaux 1-Centre National de la Recherche Scientifique (CNRS), Division of Biology [La Jolla], University of California-University of California, UMR 0441 INRA / CNRS : Laboratoire de Biologie moléculaire des relations plantes-microorganismes, Institut National de la Recherche Agronomique (INRA), Laboratoire des interactions plantes micro-organismes (LIPM), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Sexe et évolution, Département PEGASE [LBBE] (PEGASE), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Biotechnologies Végétales appliquées aux Plantes Aromatiques et Médicinales (LBVPAM), Université Jean Monnet [Saint-Étienne] (UJM), Unité de Recherche Génomique Info (URGI), Génétique Diversité et Ecophysiologie des Céréales (GDEC), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), Département de chirurgie, CRLCC Val d'Aurelle - Paul Lamarque, Génomique métabolique (UMR 8030), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Reproduction et développement des plantes (RDP), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Ecologie des Hydrosystèmes Naturels et Anthropisés (LEHNA), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-École Nationale des Travaux Publics de l'État (ENTPE)-Centre National de la Recherche Scientifique (CNRS), Centre for Plant Integrative Biology [Nothingham] (CPIB), University of Nottingham, UK (UON), Institut de Génomique d'Evry (IG), Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Institut Sophia Agrobiotech [Sophia Antipolis] (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Institut méditerranéen de biodiversité et d'écologie marine et continentale (IMBE), Avignon Université (AU)-Aix Marseille Université (AMU)-Institut de recherche pour le développement [IRD] : UMR237-Centre National de la Recherche Scientifique (CNRS), GeT PlaGe, Genotoul, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Sun Yat-Sen University [Guangzhou] (SYSU), Institut Méditerranéen d'Ecologie et de Paléoécologie (IMEP), Université Paul Cézanne - Aix-Marseille 3-Université de Provence - Aix-Marseille 1-Avignon Université (AU)-Centre National de la Recherche Scientifique (CNRS), Huazhong Agricultural University, Division of Biology [Pasadena], California Institute of Technology (CALTECH), Unité de recherche Génétique et amélioration des fruits et légumes (GAFL), Génétique et Ecophysiologie des Légumineuses à Graines (UMRLEG) (UMR 102), Etablissement National d'Enseignement Supérieur Agronomique de Dijon (ENESAD)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Universitat Politecnica de Valencia (UPV), Institute of Agrifood Research and Technology (IRTA), Institut de Recerca i Tecnologia Agroalimentaries, King Abdullah University of Science and Technology (KAUST), Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), School of Economics and Management [Beijing] (BUAA), Beihang University, Institut de biotechnologie des plantes (IBP), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), University of Warwick [Coventry], AgroParisTech, and ANR-18-CE20-0015,EPICLIPSE,Dynamique des marques épigénétiques dans les cellules hôtes infectées et subversion de l'épigénome par le pathogène.(2018)

Subjects
0106 biological sciences, Transcription, Genetic, AcademicSubjects/SCI00010, [SDV]Life Sciences [q-bio], Arabidopsis, Biology, Genes, Plant, 01 natural sciences, Histones, 03 medical and health sciences, Gene Expression Regulation, Plant, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Genetics, Homeostasis, Plant Immunity, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Epigenetics, Promoter Regions, Genetic, QH426, ComputingMilieux_MISCELLANEOUS, Histone Acetyltransferases, 030304 developmental biology, Regulation of gene expression, 0303 health sciences, Arabidopsis Proteins, Lysine, Gene regulation, Chromatin and Epigenetics, Acetylation, Biotic stress, [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics, Cell biology, Chromatin, enzymes and coenzymes (carbohydrates), Histone, Acetyltransferase, Transcription Coactivator, biology.protein, 5' Untranslated Regions, Salicylic Acid, 010606 plant biology & botany
Abstract

The modification of histones by acetyl groups has a key role in the regulation of chromatin structure and transcription. The Arabidopsis thaliana histone acetyltransferase GCN5 regulates histone modifications as part of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) transcriptional coactivator complex. GCN5 was previously shown to acetylate lysine 14 of histone 3 (H3K14ac) in the promoter regions of its target genes even though GCN5 binding did not systematically correlate with gene activation. Here, we explored the mechanism through which GCN5 controls transcription. First, we fine-mapped its GCN5 binding sites genome-wide and then used several global methodologies (ATAC-seq, ChIP-seq and RNA-seq) to assess the effect of GCN5 loss-of-function on the expression and epigenetic regulation of its target genes. These analyses provided evidence that GCN5 has a dual role in the regulation of H3K14ac levels in their 5′ and 3′ ends of its target genes. While the gcn5 mutation led to a genome-wide decrease of H3K14ac in the 5′ end of the GCN5 down-regulated targets, it also led to an increase of H3K14ac in the 3′ ends of GCN5 up-regulated targets. Furthermore, genome-wide changes in H3K14ac levels in the gcn5 mutant correlated with changes in H3K9ac at both 5′ and 3′ ends, providing evidence for a molecular link between the depositions of these two histone modifications. To understand the biological relevance of these regulations, we showed that GCN5 participates in the responses to biotic stress by repressing salicylic acid (SA) accumulation and SA-mediated immunity, highlighting the role of this protein in the regulation of the crosstalk between diverse developmental and stress-responsive physiological programs. Hence, our results demonstrate that GCN5, through the modulation of H3K14ac levels on its targets, controls the balance between biotic and abiotic stress responses and is a master regulator of plant-environmental interactions.

Published
2020
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7. EHD1 Functions in Endosomal Recycling and Confers Salt Tolerance.

Author

Bar, Maya, Leibman, Meirav, Schuster, Silvia, Pitzhadza, Hilla, and Avni, Adi

Subjects
ENDOCYTOSIS, EUKARYOTIC cells, PLANTS, ARABIDOPSIS, SEEDLINGS, SALINITY
Abstract

Endocytosis is a crucial process in all eukaryotic organisms including plants. We have previously shown that two Arabidopsis proteins, AtEHD1 and AtEHD2, are involved in endocytosis in plant systems. Knock-down of EHD1 was shown to have a delayed recycling phenotype in mammalians. There are many works in mammalian systems detailing the importance of the various domains in EHDs but, to date, the domains of plant EHD1 that are required for its activity have not been characterized. In this work we demonstrate that knock-down of EHD1 causes a delayed recycling phenotype and reduces Brefeldin A sensitivity in Arabidopsis seedlings. The EH domain of EHD1 was found to be crucial for the localization of EHD1 to endosomal structures. Mutant EHD1 lacking the EH domain did not localize to endosomal structures and showed a phenotype similar to that of EHD1 knock-down seedlings. Mutants lacking the coiled-coil domain, however, showed a phenotype similar to wild-type or EHD1 overexpression seedlings. Salinity stress is a major problem in current agriculture. Microarray data demonstrated that salinity stress enhances the expression of EHD1, and this was confirmed by semi quantitative RT-PCR. We demonstrate herein that transgenic plants over expressing EHD1 possess enhanced tolerance to salt stress, a property which also requires an intact EH domain. [ABSTRACT FROM AUTHOR]

Published
2013
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