Protein kinase associated with ribosomes of streptomycetes
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
10588047
DOI
10.1007/bf02816231
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins metabolism MeSH
- Peptide Elongation Factor Tu metabolism MeSH
- Phosphorylation MeSH
- Molecular Sequence Data MeSH
- Protein Kinases metabolism MeSH
- Ribosomal Proteins metabolism MeSH
- Ribosomes metabolism MeSH
- Amino Acid Sequence MeSH
- Streptomyces enzymology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Peptide Elongation Factor Tu MeSH
- Protein Kinases MeSH
- Ribosomal Proteins MeSH
Protein kinases can be classified into two main superfamilies on the basis of their sequence similarity and substrate specificity. The protein His kinase superfamily which autophosphorylate a His residue, and superfamily Ser/Thr and Tyr protein kinases, which phosphorylate Ser, Thr or Tyr residues. During the last years genes encoding Ser/Thr protein kinases have been identified in several microorganisms. Phosphorylation of proteins on Ser/Thr residues can be involved in many functions of prokaryotic cells including cell differentiation, signal transduction and protein biosynthesis. Phosphorylation of prokaryotic protein-synthesizing systems showed that the phosphorylation of initiation and elongation factors is subject to alteration during cell differentiation or bacteriophage infection. Protein kinase associated with ribosomes of streptomycetes phosphorylate the elongation factor Tu and 11 ribosomal proteins even in bacteriophage-uninfected cells. After phosphorylation of ribosomal proteins, ribosomes lose about 30% of their activity at the translation of poly(U).
See more in PubMed
J Biol Chem. 1972 Oct 10;247(19):6365-7 PubMed
Biochemistry. 1992 May 26;31(20):4822-7 PubMed
Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444-8 PubMed
J Bacteriol. 1977 Oct;132(1):262-9 PubMed
Mol Microbiol. 1994 Mar;11(6):1045-57 PubMed
Mol Gen Genet. 1993 Jan;236(2-3):347-54 PubMed
Biochim Biophys Acta. 1994 Oct 18;1219(2):543-7 PubMed
Mol Gen Genet. 1981;181(3):309-12 PubMed
Biochemistry. 1972 Jun 20;11(13):2503-9 PubMed
J Biol Chem. 1993 Jan 5;268(1):601-7 PubMed
Virology. 1990 Apr;175(2):525-34 PubMed
J Biol Chem. 1995 Jun 16;270(24):14541-7 PubMed
Biochem Biophys Res Commun. 1995 Aug 15;213(2):454-61 PubMed
Microbiology. 1994 Apr;140 ( Pt 4):983-98 PubMed
FEMS Microbiol Lett. 1998 Jan 1;158(1):147-51 PubMed
J Bacteriol. 1992 Apr;174(8):2474-7 PubMed
Mol Microbiol. 1997 Feb;23(3):459-71 PubMed
Evidence for phosphoprotein phosphatase in Streptomyces granaticolor
