Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective

The discovery of tyrosine-phosphorylated proteins in Bacillus subtilis in the year 2003 was followed by a decade of intensive research activity. Here we provide an overview of the lessons learned in that period. While the number of characterized kinases and phosphatases involved in reversible protei...

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Published inFrontiers in microbiology Vol. 6; no. JAN; p. 18
Main Authors Mijakovic, Ivan, Deutscher, Josef
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media 2015
Frontiers Media S.A
Subjects
BY-kinase
Life Sciences
Microbiology
phosphotyrosine-protein phosphatase
Protein phosphorylation
regulatory network
Substrate Specificity
regulatory network
protein phosphorylation
BY-kinase
substrate specificity
phosphotyrosine-protein phosphatase
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Summary:The discovery of tyrosine-phosphorylated proteins in Bacillus subtilis in the year 2003 was followed by a decade of intensive research activity. Here we provide an overview of the lessons learned in that period. While the number of characterized kinases and phosphatases involved in reversible protein-tyrosine phosphorylation in B. subtilis has remained essentially unchanged, the number of proteins known to be targeted by this post-translational modification has increased dramatically. This is mainly due to phosphoproteomics and interactomics studies, which were instrumental in identifying new tyrosine-phosphorylated proteins. Despite their structural similarity, the two B. subtilis protein-tyrosine kinases (BY-kinases), PtkA and PtkB (EpsB), seem to accomplish different functions in the cell. The PtkB is encoded by a large operon involved in exopolysaccharide production, and its main role appears to be the control of this process. The PtkA seems to have a more complex role; it phosphorylates and regulates a large number of proteins involved in the DNA, fatty acid and carbon metabolism and engages in physical interaction with other types of kinases (Ser/Thr kinases), leading to mutual phosphorylation. PtkA also seems to respond to several activator proteins, which direct its activity toward different substrates. In that respect PtkA seems to function as a highly connected signal integration device.
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This article was submitted to Microbial Physiology and Metabolism, a section of the journal Frontiers in Microbiology.
Edited by: Jörg Stülke, Georg-August-Universität Göttingen, Germany
Reviewed by: Haike Antelmann, University of Greifswald, Germany; Jörg Stülke, Georg-August-Universität Göttingen, Germany
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2015.00018