期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 4, 页码 E466-E475出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1615439114
关键词
RecQ; helicase; magnetic tweezers; single molecule; DNA unwinding
资金
- Human Frontier Science Program [RGY0072/2010]
- Hungarian Academy of Sciences Momentum Program [LP2011-006/2011]
- Eotvos Lorand University [KMOP-4.2.1/B-10-2011-0002]
- National Research, Development and Innovation Office (NKFIH) [K-116072]
- NKFIH Grant [ERC_HU 117680]
- National Heart, Lung, and Blood Institute, National Institutes of Health, Intramural Research Program [HL001056-07]
- Marie Sklodowska-Curie Reintegration Fellowship [H2020-MSCA-IF-2014-657076]
Cells must continuously repair inevitable DNA damage while avoiding the deleterious consequences of imprecise repair. Distinction between legitimate and illegitimate repair processes is thought to be achieved in part through differential recognition and processing of specific noncanonical DNA structures, although the mechanistic basis of discrimination remains poorly defined. Here, we show that Escherichia coli RecQ, a central DNA recombination and repair enzyme, exhibits differential processing of DNA substrates based on their geometry and structure. Through single-molecule and ensemble biophysical experiments, we elucidate how the conserved domain architecture of RecQ supports geometry-dependent shuttling and directed processing of recombination-intermediate [displacement loop (D-loop)] substrates. Our study shows that these activities together suppress illegitimate recombination in vivo, whereas unregulated duplex unwinding is detrimental for recombination precision. Based on these results, we propose a mechanism through which RecQ helicases achieve recombination precision and efficiency.
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