| Autor: |
Paull TT; Department of Molecular Genetics and Microbiology, University of Texas, Austin, TX 78712, USA. tpaull@icmb.utexas.edu, Cortez D, Bowers B, Elledge SJ, Gellert M |
| Jazyk: |
angličtina |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2001 May 22; Vol. 98 (11), pp. 6086-91. Date of Electronic Publication: 2001 May 15. |
| DOI: |
10.1073/pnas.111125998 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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