Journal article
Protein-Tyrosine Phosphorylation in Bacillus subtilis
In recent years bacterial protein-tyrosine kinases have been found to phosphorylate a growing number of protein substrates, including RNA polymerase sigma factors, UDP-glucose dehydrogenases and single-stranded DNA-binding proteins. The activity of these protein substrates was affected by tyrosine phosphorylation, indicating that this post-translational modifi cation could regulate physiological processes ranging from stress response and exopolysaccharide synthesis to DNA metabolism.
Some interesting work in this fi eld was done in Bacillus subtilis , and we here present the current state of knowledge on protein-tyrosine phosphorylation in this gram-positive model organism. With its two kinases, two kinase modulators, three phosphatases and at least four different tyrosine-phosphorylated substrates, B. subtilis is the bacterium with the highest number of presently known participants in the global network of protein-tyrosine phosphorylation.
We discuss the approaches currently used to chart this network: ranging from studies of substrate specifi city and the physiological role of tyrosine phosphorylation of individual enzymes to the global approaches at the level of systems biology.
Language: | English |
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Publisher: | S. Karger AG |
Year: | 2005 |
Pages: | 189-197 |
ISSN: | 16602412 , 14641801 , 14753774 , 26731673 and 26731665 |
Types: | Journal article |
DOI: | 10.1159/000089647 |
ORCIDs: | Mijakovic, Ivan and Jensen, Peter Ruhdal |
Adaptation, Physiological Bacillus subtilis Bacterial Proteins Phosphoprotein Phosphatases Phosphorylation Phosphotyrosine Phosphotyrosine-protein phosphatase Protein Processing, Post-Translational Protein phosphorylation Protein-Tyrosine Kinases Protein-tyrosine kinase Substrate specificity Systems Biology