Details
| Original language | English |
|---|---|
| Pages (from-to) | 182-188 |
| Number of pages | 7 |
| Journal | Journal of Molecular Microbiology and Biotechnology |
| Volume | 9 |
| Issue number | 3-4 |
| Publication status | Published - Jan 2006 |
| Externally published | Yes |
Abstract
A new kind of prokaryotic protein tyrosine kinase was recently discovered, utilizing a guanidino-phosphotransferase domain for its kinase activity. Guanidino kinase domains originate from eukaryotic phosphagen kinases, a family of phosphoryl transfer enzymes with no homology to the serine/threonine and tyrosine kinase superfamily. Nevertheless, this kinase, McsB, exhibits the main structural and functional properties of prokaryotic tyrosine kinases. Tyrosine phosphorylation in bacteria is predominantly described to be involved in the regulation of exopolysaccharide synthesis and is therefore required for biofilm formation and virulence. McsB on the other hand modulates together with its activator protein, McsA, the activity of the repressor of the class III heat shock genes in B. subtilis. The analogy of the kinase mechanism of McsB to tyrosine kinases implicates that tyrosine kinases may harbor various and independently evolved domains for ATP-binding/hydrolysis and the transfer of the γ-phosphate of ATP onto tyrosine residues.
Keywords
- Bacillus subtilis, Phosphagen kinase, Signal transduction, Tyrosine kinase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Immunology and Microbiology(all)
- Microbiology
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: Journal of Molecular Microbiology and Biotechnology, Vol. 9, No. 3-4, 01.2006, p. 182-188.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - A New Tyrosine Phosphorylation Mechanism Involved in Signal Transduction in Bacillus subtilis
AU - Kirstein, Janine
AU - Turgay, Kürşad
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2006/1
Y1 - 2006/1
N2 - A new kind of prokaryotic protein tyrosine kinase was recently discovered, utilizing a guanidino-phosphotransferase domain for its kinase activity. Guanidino kinase domains originate from eukaryotic phosphagen kinases, a family of phosphoryl transfer enzymes with no homology to the serine/threonine and tyrosine kinase superfamily. Nevertheless, this kinase, McsB, exhibits the main structural and functional properties of prokaryotic tyrosine kinases. Tyrosine phosphorylation in bacteria is predominantly described to be involved in the regulation of exopolysaccharide synthesis and is therefore required for biofilm formation and virulence. McsB on the other hand modulates together with its activator protein, McsA, the activity of the repressor of the class III heat shock genes in B. subtilis. The analogy of the kinase mechanism of McsB to tyrosine kinases implicates that tyrosine kinases may harbor various and independently evolved domains for ATP-binding/hydrolysis and the transfer of the γ-phosphate of ATP onto tyrosine residues.
AB - A new kind of prokaryotic protein tyrosine kinase was recently discovered, utilizing a guanidino-phosphotransferase domain for its kinase activity. Guanidino kinase domains originate from eukaryotic phosphagen kinases, a family of phosphoryl transfer enzymes with no homology to the serine/threonine and tyrosine kinase superfamily. Nevertheless, this kinase, McsB, exhibits the main structural and functional properties of prokaryotic tyrosine kinases. Tyrosine phosphorylation in bacteria is predominantly described to be involved in the regulation of exopolysaccharide synthesis and is therefore required for biofilm formation and virulence. McsB on the other hand modulates together with its activator protein, McsA, the activity of the repressor of the class III heat shock genes in B. subtilis. The analogy of the kinase mechanism of McsB to tyrosine kinases implicates that tyrosine kinases may harbor various and independently evolved domains for ATP-binding/hydrolysis and the transfer of the γ-phosphate of ATP onto tyrosine residues.
KW - Bacillus subtilis
KW - Phosphagen kinase
KW - Signal transduction
KW - Tyrosine kinase
UR - http://www.scopus.com/inward/record.url?scp=30744470097&partnerID=8YFLogxK
U2 - 10.1159/000089646
DO - 10.1159/000089646
M3 - Review article
C2 - 16415591
AN - SCOPUS:30744470097
VL - 9
SP - 182
EP - 188
JO - Journal of Molecular Microbiology and Biotechnology
JF - Journal of Molecular Microbiology and Biotechnology
SN - 1464-1801
IS - 3-4
ER -