Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase α subunit C-terminal domain complex

被引:26
作者
Lamour, Valerie [1 ,2 ]
Westblade, Lars F. [1 ]
Campbell, Elizabeth A. [1 ]
Darst, Seth A. [1 ]
机构
[1] Rockefeller Univ, Lab Mol Biophys, New York, NY 10065 USA
[2] IGBMC, F-67404 Illkirch Graffenstaden, France
关键词
Bacillus subtillus; Spx; RNA polymerase; Transcription; COLI RNA-POLYMERASE; GLOBAL TRANSCRIPTIONAL CONTROL; ORGANOSULFUR METABOLISM; DEPENDENT PROMOTERS; DNA-BINDING; PROTEIN; SPX; IDENTIFICATION; ELEMENT; DETERMINANTS;
D O I
10.1016/j.jsb.2009.07.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Bacillus subtilis Spx protein is a global transcription factor that interacts with the C-terminal domain of the RNA polymerase alpha subunit (alpha CTD) and regulates transcription of genes involved in thiol-oxidative stress, sporulation, competence, and organosulfur metabolism. Here we determined the X-ray crystal structure of the Spx/alpha CTD complex from an entirely new crystal form than previously reported [Newberry, K.J., Nakano, S., Zuber, P., Brennan, R.G., 2005. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc. Natl. Acad. Sci. USA 102, 15839-15844]. Comparison of the previously reported sulfate-bound complex and our sulfate-free complex reveals subtle conformational changes that may be important for the role of Spx in regulating organosulfur metabolism. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:352 / 356
页数:5
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