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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : The Biochemical journal

The stress sigma factor of RNA polymerase RpoS/σ is a solvent-exposed open molecule in solution

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Biochemical journal - 15 Jan 2018

Cavaliere P, Brier S, Filipenko P, Sizun C, Raynal B, Bonneté F, Levi-Acobas F, Bellalou J, England P, Chamot-Rooke J, Mayer C, Norel F

Link to Pubmed [PMID] – 29229758

Biochem. J. 2018 01;475(1):341-354

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 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 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 Instead, we show that σ adopts an open conformation in solution in which the folded σ and σ 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 and provide insights into the possible mechanisms of regulation of σ activity by its chaperone Crl.

https://www.ncbi.nlm.nih.gov/pubmed/29229758