Mechanistic Insights into RAD51-associated Protein 1 (RAD51AP1) Action in Homologous DNA Repair
Mechanistic Insights into RAD51-associated Protein 1 (RAD51AP1) Action in Homologous DNA Repair
Homologous recombination catalyzed by the RAD51 recombinase is essential for maintaining genome integrity upon the induction of DNA double strand breaks and other DNA lesions. By enhancing the recombinase activity of RAD51, RAD51AP1 (RAD51-associated protein 1) serves a key role in homologous recombination-mediated chromosome damage repair. We show here that RAD51AP1 harbors two distinct DNA binding domains that are both needed for maximal protein activity under physiological conditions. We have finely mapped the two DNA binding domains in RAD51AP1 and generated mutant variants that are impaired in either or both of the DNA binding domains. Examination of these mutants reveals that both domains are indispensable for RAD51AP1 function in cells. These and other results illuminate the mechanistic basis of RAD51AP1 action in homologous DNA repair.
- University of Queensland Australia
- University of Queensland Australia
- Queensland University of Technology Australia
- Yale University United States
- Lawrence Berkeley National Laboratory United States
1303 Biochemistry, DNA Repair, RNA-Binding Proteins, 612, DNA, Peptide Mapping, Peptide Fragments, Recombinant Proteins, Protein Structure, Tertiary, 1307 Cell Biology, DNA-Binding Proteins, Phenotype, Amino Acid Substitution, 1312 Molecular Biology, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Conserved Sequence, HeLa Cells, Protein Binding, Sequence Deletion
1303 Biochemistry, DNA Repair, RNA-Binding Proteins, 612, DNA, Peptide Mapping, Peptide Fragments, Recombinant Proteins, Protein Structure, Tertiary, 1307 Cell Biology, DNA-Binding Proteins, Phenotype, Amino Acid Substitution, 1312 Molecular Biology, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Conserved Sequence, HeLa Cells, Protein Binding, Sequence Deletion
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