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

Frontiers in Microbiology

卷:6

Ivan eMijakovic¹  Josef eDeutscher² 

[1] Chalmers University of Technology;

[2] Institut National de la Recherche Agronomique/AgroParisTech;

关键词: Substrate Specificity;    Protein phosphorylation;    regulatory network;    BY-kinase;    phosphotyrosine-protein phosphatase;   

DOI  :  10.3389/fmicb.2015.00018

来源: DOAJ

【 摘 要 】

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 towards different substrates. In that respect PtkA seems to function as a highly connected signal integration device.

【 授权许可】

Unknown