Alternative Sigma Factors in the Free State Are Equilibrium Mixtures of Open and Compact Conformations
Author:
Affiliation:
1. Department of Structural Biology and Bioinformatics, Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700 032, India
2. Department of Biophysics, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700 054, India
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1011173
Reference30 articles.
1. Amino-terminal amino acids modulate sigma-factor DNA-binding activity.
2. Polypeptides containing highly conserved regions of transcription initiation factor σ70 exhibit specificity of binding to promoter DNA
3. Autoregulation of a bacterial factor explored by using segmental isotopic labeling and NMR
4. A Full-Length Group 1 Bacterial Sigma Factor Adopts a Compact Structure Incompatible with DNA Binding
5. Disulfide cross-linking indicates that FlgM-bound and free 28 adopt similar conformations
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1. The core-independent promoter-specific binding ofBacillus subtilisσB;FEBS Journal;2015-03-07
2. Conformational Adaptation in the E. coli Sigma 32 Protein in Response to Heat Shock;The Journal of Physical Chemistry B;2014-04-25
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