期刊
FEBS LETTERS
卷 585, 期 14, 页码 2313-2317出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.05.064
关键词
RNase H; Bacillus stearothermophilus; TATA-box binding protein; Substrate binding; Site-directed mutagenesis
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [21380065]
- New Energy and Industrial Technology Development Organization of Japan
- Grants-in-Aid for Scientific Research [21380065] Funding Source: KAKEN
Ribonuclease H3 from Bacillus stearothermophilus (Bst-RNase H3) has the N-terminal TBP-like substrate-binding domain. To identify the substrate binding site in this domain, the mutant proteins of the intact protein and isolated N-domain, in which six of the seventeen residues corresponding to those involved in DNA binding of TBP are individually mutated to Ala, were constructed. All of them exhibited decreased enzymatic activities and/or substrate-binding affinities when compared to those of the parent proteins, suggesting that the N-terminal domain of RNase H3 uses the flat surface of the beta-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. 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