A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Janine Kirstein
  • Daniela Zühlke
  • Ulf Gerth
  • Kürşad Turgay
  • Michael Hecker

Externe Organisationen

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

Details

OriginalspracheEnglisch
Seiten (von - bis)3435-3445
Seitenumfang11
FachzeitschriftEMBO Journal
Jahrgang24
Ausgabenummer19
PublikationsstatusVeröffentlicht - 5 Okt. 2005
Extern publiziertJa

Abstract

The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.

Zitieren

A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis. / Kirstein, Janine; Zühlke, Daniela; Gerth, Ulf et al.
in: EMBO Journal, Jahrgang 24, Nr. 19, 05.10.2005, S. 3435-3445.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Kirstein J, Zühlke D, Gerth U, Turgay K, Hecker M. A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis. EMBO Journal. 2005 Okt 5;24(19):3435-3445. doi: 10.1038/sj.emboj.7600780
Kirstein, Janine ; Zühlke, Daniela ; Gerth, Ulf et al. / A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis. in: EMBO Journal. 2005 ; Jahrgang 24, Nr. 19. S. 3435-3445.
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abstract = "The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.",
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T1 - A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis

AU - Kirstein, Janine

AU - Zühlke, Daniela

AU - Gerth, Ulf

AU - Turgay, Kürşad

AU - Hecker, Michael

N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2005/10/5

Y1 - 2005/10/5

N2 - The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.

AB - The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.

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