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FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination
by
Choinard, Sandrine
, Froger, Nicole
, Andrey, Philippe
, Guérois, Raphaël
, Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)
, Grelon, Mathilde
, Mercier, Raphaël
, Assemblage moléculaire et intégrité du génome (AMIG) ; Département Biochimie, Biophysique et Biologie Structurale (B3S) ; Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique e
in
Arabidopsis
/ Arabidopsis Proteins
/ Arabidopsis thaliana
/ ATPases Associated with Diverse Cellular Activities
/ Bioinformatics
/ Biology
/ Biology and Life Sciences
/ Biotechnology
/ Cancer
/ Cell Cycle Proteins
/ Chromosomes
/ Computer and Information Sciences
/ Deoxyribonucleic acid
/ DNA
/ DNA damage
/ DNA repair
/ Genetic aspects
/ Genetic crosses
/ Genetic diversity
/ Genetic recombination
/ Homologous Recombination
/ Life Sciences
/ Meiosis
/ Microtubule-Associated Proteins
/ Multiprotein Complexes
/ Mutation
/ Nuclear Proteins
/ Observations
/ Phenotypes
/ Phylogeny
/ Protein Binding
/ Protein interaction
/ Protein-protein interactions
/ Proteins
/ Rad51 Recombinase
/ Rec A Recombinases
/ Research and Analysis Methods
/ Two-Hybrid System Techniques
2018
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FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination
by
Choinard, Sandrine
, Froger, Nicole
, Andrey, Philippe
, Guérois, Raphaël
, Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)
, Grelon, Mathilde
, Mercier, Raphaël
, Assemblage moléculaire et intégrité du génome (AMIG) ; Département Biochimie, Biophysique et Biologie Structurale (B3S) ; Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique e
in
Arabidopsis
/ Arabidopsis Proteins
/ Arabidopsis thaliana
/ ATPases Associated with Diverse Cellular Activities
/ Bioinformatics
/ Biology
/ Biology and Life Sciences
/ Biotechnology
/ Cancer
/ Cell Cycle Proteins
/ Chromosomes
/ Computer and Information Sciences
/ Deoxyribonucleic acid
/ DNA
/ DNA damage
/ DNA repair
/ Genetic aspects
/ Genetic crosses
/ Genetic diversity
/ Genetic recombination
/ Homologous Recombination
/ Life Sciences
/ Meiosis
/ Microtubule-Associated Proteins
/ Multiprotein Complexes
/ Mutation
/ Nuclear Proteins
/ Observations
/ Phenotypes
/ Phylogeny
/ Protein Binding
/ Protein interaction
/ Protein-protein interactions
/ Proteins
/ Rad51 Recombinase
/ Rec A Recombinases
/ Research and Analysis Methods
/ Two-Hybrid System Techniques
2018
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FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination
by
Choinard, Sandrine
, Froger, Nicole
, Andrey, Philippe
, Guérois, Raphaël
, Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)
, Grelon, Mathilde
, Mercier, Raphaël
, Assemblage moléculaire et intégrité du génome (AMIG) ; Département Biochimie, Biophysique et Biologie Structurale (B3S) ; Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC) ; Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique e
in
Arabidopsis
/ Arabidopsis Proteins
/ Arabidopsis thaliana
/ ATPases Associated with Diverse Cellular Activities
/ Bioinformatics
/ Biology
/ Biology and Life Sciences
/ Biotechnology
/ Cancer
/ Cell Cycle Proteins
/ Chromosomes
/ Computer and Information Sciences
/ Deoxyribonucleic acid
/ DNA
/ DNA damage
/ DNA repair
/ Genetic aspects
/ Genetic crosses
/ Genetic diversity
/ Genetic recombination
/ Homologous Recombination
/ Life Sciences
/ Meiosis
/ Microtubule-Associated Proteins
/ Multiprotein Complexes
/ Mutation
/ Nuclear Proteins
/ Observations
/ Phenotypes
/ Phylogeny
/ Protein Binding
/ Protein interaction
/ Protein-protein interactions
/ Proteins
/ Rad51 Recombinase
/ Rec A Recombinases
/ Research and Analysis Methods
/ Two-Hybrid System Techniques
2018
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FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination
Journal Article
FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination
2018
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Overview
Homologous recombination is central to repair DNA double-strand breaks, either accidently arising in mitotic cells or in a programed manner at meiosis. Crossovers resulting from the repair of meiotic breaks are essential for proper chromosome segregation and increase genetic diversity of the progeny. However, mechanisms regulating crossover formation remain elusive. Here, we identified through genetic and protein-protein interaction screens FIDGETIN-LIKE-1 INTERACTING PROTEIN (FLIP) as a new partner of the previously characterized anti-crossover factor FIDGETIN-LIKE-1 (FIGL1) in Arabidopsis thaliana. We showed that FLIP limits meiotic crossover together with FIGL1. Further, FLIP and FIGL1 form a protein complex conserved from Arabidopsis to human. FIGL1 interacts with the recombinases RAD51 and DMC1, the enzymes that catalyze the DNA strand exchange step of homologous recombination. Arabidopsis flip mutants recapitulate the figl1 phenotype, with enhanced meiotic recombination associated with change in counts of DMC1 and RAD51 foci. Our data thus suggests that FLIP and FIGL1 form a conserved complex that regulates the crucial step of strand invasion in homologous recombination.
Publisher
Public Library of Science,CCSD,Public Library of Science (PLoS)
Subject
ISBN
0004311157000
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