Regulation of Rad51 function by phosphorylation

Autor: Stephen P. Jackson, Phoebe A. Rice, Sonja Flott, Ying Z. Pigli, Youngho Kwon, Patrick Sung
Rok vydání: 2011
Předmět:
Models
Molecular
Saccharomyces cerevisiae Proteins
DNA Repair
DNA repair
DNA damage
Molecular Sequence Data
genetic processes
Saccharomyces cerevisiae
RAD51
Protein Serine-Threonine Kinases
Biology
medicine.disease_cause
Biochemistry
chemistry.chemical_compound
Adenosine Triphosphate
Genetics
medicine
DNA Breaks
Double-Stranded
Amino Acid Sequence
Phosphorylation
Molecular Biology
Adenosine Triphosphatases
Recombination
Genetic
Mutation
Sequence Homology
Amino Acid
Hydrolysis
Scientific Reports
Intracellular Signaling Peptides and Proteins
biology.organism_classification
Molecular biology
DNA-Binding Proteins
enzymes and coenzymes (carbohydrates)
chemistry
health occupations
Rad51 Recombinase
biological phenomena
cell phenomena
and immunity
Homologous recombination
Adenosine triphosphate
DNA
Zdroj: EMBO reports. 12:833-839
ISSN: 1469-3178
1469-221X
DOI: 10.1038/embor.2011.127
Popis: Rad51 is a key enzyme involved in DNA double-strand break repair by homologous recombination. Here, we show that in response to DNA damage, budding yeast Rad51 is phosphorylated on Ser 192 in a manner that is primarily mediated by the DNA-damage-responsive protein kinase Mec1. We show that mutating Rad51 Ser 192 to Ala or Glu confers hypersensitivity to DNA damage and homologous-recombination defects. Furthermore, biochemical analyses indicate that Ser 192 is required for Rad51 adenosine triphosphate hydrolysis and DNA-binding activity in vitro, whereas mutation of Ser 192 does not interfere with Rad51 multimer formation. These data suggest a model in which Mec1-mediated phosphorylation of Rad51 Ser 192 in response to DNA damage controls Rad51 activity and DNA repair by homologous recombination.
Databáze: OpenAIRE
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