McsB Is a Protein Arginine Kinase That Phosphorylates and Inhibits the Heat-Shock Regulator CtsR

Author:

Fuhrmann Jakob1,Schmidt Andreas2,Spiess Silvia3,Lehner Anita1,Turgay Kürşad4,Mechtler Karl15,Charpentier Emmanuelle36,Clausen Tim1

Affiliation:

1. Research Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria.

2. Christian Doppler Laboratory for Proteome Analysis, University of Vienna, Dr. Bohrgasse 3, A-1030 Vienna, Austria.

3. Max F. Perutz Laboratories, University of Vienna, Dr. Bohrgasse 9, A-1030 Vienna, Austria.

4. Institute for Biology–Microbiology, Freie Universität Berlin, Königin-Luisé-Str. 12-16, 14195 Berlin, Germany.

5. Institute for Molecular Biotechnology–IMBA, Dr. Bohrgasse 3, A-1030 Vienna, Austria.

6. The Laboratory for Molecular Infection Medicine Sweden, Umeå University, S-90187 Umeå, Sweden.

Abstract

Transcriptional Repressor Dissected Living organisms have quality-control mechanisms to eliminate proteins damaged by environmental stresses. In the model organism Bacillus subtilis , the transcriptional repressor CtsR controls the expression of genes that are key to the heat-shock response. CtsR is activated by the kinase McsB to allow transcription of stress response genes, however, the mechanism of activation is unclear. Fuhrmann et al. (p. 1323 ) now describe structural and biochemical studies showing that McsB inhibits DNA binding of CtsR by specifically phosphorylating arginine residues in its DNA binding domain. This study provides a basis for exploring a potential wider role of arginine phosphorylation in prokaryotic and eukaryotic transcriptional regulation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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