Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex.
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.
Lamour
Valerie
V
The Rockefeller University, New York, NY 10065, USA.
Westblade
Lars F
LF
Campbell
Elizabeth A
EA
Darst
Seth A
SA
D001412:Bacillus subtilis / Q000201:enzymology*; D018360:Crystallography, X-Ray / Q000379:methods*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D017433:Protein Structure, Secondary
D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit