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

Abstract : The Bacillus subtilis Spx protein is a global transcription factor that interacts with the C-terminal domain of the RNA polymerase alpha subunit (alphaCTD) 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/alphaCTD 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.
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Journal of Structural Biology, Elsevier, 2009, 168 (2), pp.352-6. 〈10.1016/j.jsb.2009.07.001〉
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Soumis le : vendredi 4 décembre 2009 - 11:45:25
Dernière modification le : jeudi 15 mars 2018 - 01:33:23

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Valerie Lamour, Lars Westblade, Elizabeth Campbell, Seth Darst. Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex.. Journal of Structural Biology, Elsevier, 2009, 168 (2), pp.352-6. 〈10.1016/j.jsb.2009.07.001〉. 〈inserm-00438652〉

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