期刊
SCIENCE IN CHINA SERIES C-LIFE SCIENCES
卷 52, 期 11, 页码 997-1002出版社
SCIENCE PRESS
DOI: 10.1007/s11427-009-0141-1
关键词
RbsD; oligomeric protein; oligomeric intermediate; refolding; reassembly
类别
资金
- National Natural Science Foundation of China [30570355, 30670022, 30870055]
- National Key Basic Research Foundation of China [2006CB806508, 2006CB910300]
Many proteins exist as homo-oligomers in living organisms wherein the change of oligomeric status apparently serves as an effective means for modulating their biological activities. We have previously reported that the homo-decameric RbsD from Escherichia coli undergoes stepwise disassembly and non-stepwise reassembly. Here the structural status of the urea-induced RbsD disassembly intermediates was examined, mainly using urea-containing polyacrylamide gel electrophoresis and chemical cross-linking. Such intermediates were found to remain oligomeric while losing their intact secondary structures. Such disassembly intermediates were able to effectively refold when the concentration of the urea denaturant was reduced to a lower level, or to refold/reassemble into the native decamers when urea was completely removed, as detected by non-denaturing polyacrylamide gel electrophoresis. These novel observations strongly suggest that the assembly of oligomeric proteins may occur before the completion of subunit folding.
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