David Cortez
Faculty Member
Last active: 2/4/2016

Direct DNA binding by Brca1.

Paull TT, Cortez D, Bowers B, Elledge SJ, Gellert M
Proc Natl Acad Sci U S A. 2001 98 (11): 6086-91

PMID: 11353843 · PMCID: PMC33426 · DOI:10.1073/pnas.111125998

The tumor suppressor Brca1 plays an important role in protecting mammalian cells against genomic instability, but little is known about its modes of action. In this work we demonstrate that recombinant human Brca1 protein binds strongly to DNA, an activity conferred by a domain in the center of the Brca1 polypeptide. As a result of this binding, Brca1 inhibits the nucleolytic activities of the Mre11/Rad50/Nbs1 complex, an enzyme implicated in numerous aspects of double-strand break repair. Brca1 displays a preference for branched DNA structures and forms protein-DNA complexes cooperatively between multiple DNA strands, but without DNA sequence specificity. This fundamental property of Brca1 may be an important part of its role in DNA repair and transcription.

MeSH Terms (15)

Animals Binding Sites BRCA1 Protein Cell Cycle Proteins DNA DNA-Binding Proteins DNA Damage DNA Repair Exodeoxyribonucleases Genes, Tumor Suppressor Humans MRE11 Homologue Protein Nuclear Proteins Protein Binding Recombinant Fusion Proteins

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