Journal article
Bacillus subtilis Two-Component System Sensory Kinase DegS Is Regulated by Serine Phosphorylation in Its Input Domain
Department of Chemical and Biochemical Engineering, Technical University of Denmark1
Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark2
AgroParisTech3
Department of Systems Biology, Technical University of Denmark4
Center for Microbial Biotechnology, Department of Systems Biology, Technical University of Denmark5
Center for Systems Microbiology, Department of Systems Biology, Technical University of Denmark6
Bacillus subtilis two-component system DegS/U is well known for the complexity of its regulation. The cytosolic sensory kinase DegS does not receive a single predominant input signal like most two-component kinases, instead it integrates a wide array of metabolic inputs that modulate its activity. The phosphorylation state of the response regulator DegU also does not confer a straightforward "on/off" response; it is fine-tuned and at different levels triggers different sub-regulons.
Here we describe serine phosphorylation of the DegS sensing domain, which stimulates its kinase activity. We demonstrate that DegS phosphorylation can be carried out by at least two B. subtilis Hanks-type kinases in vitro, and this stimulates the phosphate transfer towards DegU. The consequences of this process were studied in vivo, using phosphomimetic (Ser76Asp) and non-phosphorylatable (Ser76Ala) mutants of DegS.
In a number of physiological assays focused on different processes regulated by DegU, DegS S76D phosphomimetic mutant behaved like a strain with intermediate levels of DegU phosphorylation, whereas DegS S76A behaved like a strain with lower levels of DegU phophorylation. These findings suggest a link between DegS phosphorylation at serine 76 and the level of DegU phosphorylation, establishing this post-translational modification as an additional trigger for this two-component system.
Language: | English |
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Publisher: | Public Library of Science |
Year: | 2011 |
Pages: | e14653 |
ISSN: | 19326203 |
Types: | Journal article |
DOI: | 10.1371/journal.pone.0014653 |
ORCIDs: | Jers, Carsten and Jensen, Peter Ruhdal |
Bacillus subtilis Bacterial Proteins Catalytic Domain Colony Count, Microbial DegS protein, Bacteria DegU protein, Bacteria Medicine Mutant Proteins Organisms, Genetically Modified Phosphorylation Phosphotransferases Protein Processing, Post-Translational Protein Structure, Tertiary Q R Science Serine Time Factors