期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 312, 期 5, 页码 949-962出版社
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2001.4941
关键词
transcription; recombination; trimer; bending; analytical ultracentrifugation
Allosteric activation of the hexameric arginine repressor (ArgR) for specific operator DNA binding appears to involve alteration in its quaternary structure. Current models for activation include subunit assembly and/or domain rearrangements in response to binding of the coeffector L-arginine. To investigate the molecular basis for ArgR operator interactions we have carried out a series of quantitative analyses of ArgR subunit assembly and of the affinity, stoichiometry, cooperativity, and L-arginine- and DNA sequence-dependence of ArgR-DNA binding. The results indicate that subunit assembly plays no role in although communication among subunits of the ArgR hexamer is required for specific DNA binding. The data suggest that DNA is also an allosteric effector of ArgR. (C) 2001 Academic Press.
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