The Bacillus subtilis RNA helicase YxiN is distended in solution

Shuying Wang, Michael T. Overgaard, Yao Xiong Hu, David B. McKay

研究成果: Article同行評審

23 引文 斯高帕斯(Scopus)

摘要

The Bacillus subtilis YxiN protein is a modular three-domain RNA helicase of the DEx(D/H)-box protein family. The first two domains form the highly conserved helicase core, and the third domain confers RNA target binding specificity. Small angle x-ray scattering on YxiN and two-domain fragments thereof shows that the protein has a distended structure in solution, in contrast to helicases involved in replication processes. These data are consistent with a chaperone activity in which the carboxy-terminal domain of YxiN tethers the protein to the vicinity of its targets and the helicase core is free to transiently interact with RNA duplexes, possibly to melt out misfolded elements of secondary structure.

原文English
頁(從 - 到)L01-L03
期刊Biophysical Journal
94
發行號1
DOIs
出版狀態Published - 2008 1月 1

All Science Journal Classification (ASJC) codes

  • 生物物理學

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