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

Paola Cavaliere 1 Sebastien Brier 2, 3 Petr Filipenko 4 Christina Sizun 5 Bertrand Raynal 6 Françoise Bonneté 7 Fabienne Levi-Acobas 8 Jacques Bellalou 8 Patrick England 6 Julia Chamot-Rooke 2 Claudine Mayer 9 Françoise Norel 1, 10
1 Systèmes macromoléculaires et Signalisation
2 Spectrométrie de Masse structurale et protéomique
3 UTechS MSBio - Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology
4 Department of Computer Science [New York]
5 ICSN - Institut de Chimie des Substances Naturelles
6 Biophysique Moléculaire (Plate-forme)
7 IBMM - Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]
8 PRPF - Production de Protéines Recombinantes (Plate-Forme)
9 Microb. Struc. (UMR_3528 / U-Pasteur_5) - Microbiologie structurale - Structural Microbiology
10 Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions
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.
Keywords : protein structure sigma factor protein conformation Salmonella RpoS RNA polymerase
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01685123
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Submitted on : Tuesday, January 16, 2018 - 10:12:14 AM
Last modification on : Wednesday, January 19, 2022 - 1:44:01 PM
Long-term archiving on: : Sunday, May 6, 2018 - 2:34:25 PM

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PASTEUR | CNRS | ICSN | INC-CNRS | CHIMIE | UNIV-MONTPELLIER | UNIV-PARIS7 | USPC | UNIV-PARIS | UP-SCIENCES | ANR | GS-CHIMIE | GS-HEALTH-DRUG-SCIENCES

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Paola Cavaliere, Sebastien Brier, Petr Filipenko, Christina Sizun, Bertrand Raynal, et al.. The stress sigma factor of RNA polymerase RpoS/σ S is a solvent-exposed open molecule in solution. Biochemical Journal, Portland Press, 2018, 475 (1), pp.341 - 354. ⟨10.1042/BCJ20170768⟩. ⟨pasteur-01685123⟩

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