 |
Journal articles
The stress sigma factor of RNA polymerase RpoS/σ S is a solvent-exposed open molecule in solution
Abstract : In bacteria, one primary and multiple alternative sigma (σ) factors associate with the RNA polymerase core enzyme (E) to form holoenzymes (Eσ) with different promoter recognition specificities. The alternative σ factor RpoS/σ S is produced in stationary phase and under stress conditions and reprograms global gene expression to promote bacterial survival. To date, the three-dimensional structure of a full-length free σ factor remains elusive. The current model suggests that extensive interdomain contacts in a free σ factor result in a compact conformation that masks the DNA-binding determinants of σ, explaining why a free σ factor does not bind double-stranded promoter DNA efficiently. Here, we explored the solution conformation of σ S using amide hydrogen/deuterium exchange coupled with mass spectrometry, NMR, analytical ultracentrifugation and molecular dynamics. Our data strongly argue against a compact conformation of free σ S. Instead, we show that σ S adopts an open conformation in solution in which the folded σ 2 and σ 4 domains are interspersed by domains with a high degree of disorder. These findings suggest that E binding induces major changes in both the folding and domain arrangement of σ S and provide insights into the possible mechanisms of regulation of σ S activity by its chaperone Crl.
https://hal-pasteur.archives-ouvertes.fr/pasteur-01685123
Contributor : Bénédicte Benedic <>
Submitted on : Tuesday, January 16, 2018 - 10:12:14 AM
Last modification on : Monday, May 31, 2021 - 4:44:02 PM
Long-term archiving on: : Sunday, May 6, 2018 - 2:34:25 PM
Contributor : Bénédicte Benedic <>
Submitted on : Tuesday, January 16, 2018 - 10:12:14 AM
Last modification on : Monday, May 31, 2021 - 4:44:02 PM
Long-term archiving on: : Sunday, May 6, 2018 - 2:34:25 PM
Files
Licence
Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives 4.0 International License