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

Ivan Mijakovic (Institutionen för biologi och bioteknik, Systembiologi) ; J. Deutscher
Frontiers in Microbiology (1664-302X). Vol. 6 (2015), p. Art. no. 18.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: protein phosphorylation, BY-kinase, phosphotyrosine-protein phosphatase, regulatory network, substrate specificity

Denna post skapades 2015-03-11. Senast ändrad 2015-07-07.
CPL Pubid: 213665


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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Systembiologi


Bioinformatik och systembiologi

Chalmers infrastruktur