期刊
NUCLEIC ACIDS RESEARCH
卷 40, 期 9, 页码 3952-3963出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks008
关键词
-
资金
- Norway Grants [NNF2-85613]
- Hungarian Scientific Research Fund [K71915, NK81950]
- TAMOP [4.2.1/B-09/1/KMR-2010-0003]
- Human Frontier Science Program [RGY0072/2010]
- Hungarian Academy of Sciences [LP2011-006/2011]
Bloom's syndrome DNA helicase (BLM), a member of the RecQ family, is a key player in homologous recombination (HR)-based error-free DNA repair processes. During HR, BLM exerts various biochemical activities including single-stranded (ss) DNA translocation, separation and annealing of complementary DNA strands, disruption of complex DNA structures (e.g. displacement loops) and contributes to quality control of HR via clearance of Rad51 nucleoprotein filaments. We performed a quantitative mechanistic analysis of truncated BLM constructs that are shorter than the previously identified minimal functional module. Surprisingly, we found that a BLM construct comprising only the two conserved RecA domains and the Zn2+-binding domain (residues 642-1077) can efficiently perform all mentioned HR-related activities. The results demonstrate that the Zn2+-binding domain is necessary for functional interaction with DNA. We show that the extensions of this core, including the winged-helix domain and the strand separation hairpin identified therein in other RecQ-family helicases, are not required for mechanochemical activity per se and may instead play modulatory roles and mediate protein-protein interactions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据