Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Noël Molière
  • Jörn Hoßmann
  • Heinrich Schäfer
  • Kürsad Turgay

Organisationseinheiten

Externe Organisationen

  • Freie Universität Berlin (FU Berlin)
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Aufsatznummer315
FachzeitschriftFrontiers in microbiology
Jahrgang7
AusgabenummerMAR
PublikationsstatusVeröffentlicht - 16 März 2016

Abstract

The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response, and motility. Here we analyzed the role of regulatory proteolysis by ClpXP and ClpCP in motility development. We have demonstrated that ClpXP acts on the regulation of motility by controlling the levels of the oxidative and heat stress regulator Spx. We obtained evidence that upon oxidative stress Spx not only induces the thiol stress response, but also transiently represses the transcription of flagellar genes. Furthermore, we observed that in addition to the known impact of ClpCP via the ComK/FlgM-dependent pathway, ClpCP also affects flagellar gene expression via modulating the activity and levels of the global regulator DegU-P. This adds another layer to the intricate involvement of Clp mediated regulatory proteolysis in different gene expression programs, which may allow to integrate and coordinate different signals for a better-adjusted response to the changing environment of B. subtilis cells.

ASJC Scopus Sachgebiete

Zitieren

Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis. / Molière, Noël; Hoßmann, Jörn; Schäfer, Heinrich et al.
in: Frontiers in microbiology, Jahrgang 7, Nr. MAR, 315, 16.03.2016.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Molière N, Hoßmann J, Schäfer H, Turgay K. Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis. Frontiers in microbiology. 2016 Mär 16;7(MAR):315. doi: 10.3389/fmicb.2016.00315
Molière, Noël ; Hoßmann, Jörn ; Schäfer, Heinrich et al. / Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis. in: Frontiers in microbiology. 2016 ; Jahrgang 7, Nr. MAR.
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abstract = "The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response, and motility. Here we analyzed the role of regulatory proteolysis by ClpXP and ClpCP in motility development. We have demonstrated that ClpXP acts on the regulation of motility by controlling the levels of the oxidative and heat stress regulator Spx. We obtained evidence that upon oxidative stress Spx not only induces the thiol stress response, but also transiently represses the transcription of flagellar genes. Furthermore, we observed that in addition to the known impact of ClpCP via the ComK/FlgM-dependent pathway, ClpCP also affects flagellar gene expression via modulating the activity and levels of the global regulator DegU-P. This adds another layer to the intricate involvement of Clp mediated regulatory proteolysis in different gene expression programs, which may allow to integrate and coordinate different signals for a better-adjusted response to the changing environment of B. subtilis cells.",
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AU - Molière, Noël

AU - Hoßmann, Jörn

AU - Schäfer, Heinrich

AU - Turgay, Kürsad

N1 - Publisher Copyright: © 2016 Molière, Hoßmann, Schäfer and Turgay. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.

PY - 2016/3/16

Y1 - 2016/3/16

N2 - The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response, and motility. Here we analyzed the role of regulatory proteolysis by ClpXP and ClpCP in motility development. We have demonstrated that ClpXP acts on the regulation of motility by controlling the levels of the oxidative and heat stress regulator Spx. We obtained evidence that upon oxidative stress Spx not only induces the thiol stress response, but also transiently represses the transcription of flagellar genes. Furthermore, we observed that in addition to the known impact of ClpCP via the ComK/FlgM-dependent pathway, ClpCP also affects flagellar gene expression via modulating the activity and levels of the global regulator DegU-P. This adds another layer to the intricate involvement of Clp mediated regulatory proteolysis in different gene expression programs, which may allow to integrate and coordinate different signals for a better-adjusted response to the changing environment of B. subtilis cells.

AB - The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response, and motility. Here we analyzed the role of regulatory proteolysis by ClpXP and ClpCP in motility development. We have demonstrated that ClpXP acts on the regulation of motility by controlling the levels of the oxidative and heat stress regulator Spx. We obtained evidence that upon oxidative stress Spx not only induces the thiol stress response, but also transiently represses the transcription of flagellar genes. Furthermore, we observed that in addition to the known impact of ClpCP via the ComK/FlgM-dependent pathway, ClpCP also affects flagellar gene expression via modulating the activity and levels of the global regulator DegU-P. This adds another layer to the intricate involvement of Clp mediated regulatory proteolysis in different gene expression programs, which may allow to integrate and coordinate different signals for a better-adjusted response to the changing environment of B. subtilis cells.

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