期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 384, 期 5, 页码 1273-1286出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.10.017
关键词
single molecule; enzyme disorder; translocase; helicase; ATPase
资金
- Wellcome Trust [084086, 067439]
- Grant Agency of the Czech Republic [204/07/0325]
- European Commission [043288]
- Netherlands Organization for Scientific Research
- Deutsche Forschungsgemeinschaft
The type I restriction-modification enzyme EcoR1241 comprises three subunits with the stoichiometry HsdR(2)/HsdM(2)/HsdS(1). The HsdR subunits are archetypical examples of the fusion between nuclease and helicase domains into a single polypeptide, a linkage that is found in a great many other DNA processing enzymes. To explore the interrelationship between these physically linked domains, we examined the DNA translocation properties of EcoR124I complexes in which the HsdR subunits had been mutated in the RecB-like nuclease motif II or III. We found that nuclease mutations can have multiple effects on DNA translocation despite being distinct from the helicase domain. In addition to reductions in DNA cleavage activity, we also observed decreased translocation and ATPase rates, different enzyme populations with different characteristic translocation rates, a tendency to stall during initiation and altered HsdR turnover dynamics. The significance of these observations to our understanding of domain interactions in molecular machines is discussed. (C) 2008 Elsevier Ltd. All rights reserved.
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