Effect of protein phosphorylation on the activity of RNA polymerase in streptomycetes
Language English Country United States Media print
Document type Journal Article
PubMed
1505864
DOI
10.1007/bf02814581
Knihovny.cz E-resources
- MeSH
- DNA-Directed RNA Polymerases metabolism MeSH
- Phosphorylation MeSH
- Transcription, Genetic physiology MeSH
- Protein Kinases physiology MeSH
- Streptomyces enzymology genetics MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- DNA-Directed RNA Polymerases MeSH
- Protein Kinases MeSH
RNA polymerase was isolated from Streptomyces granaticolor and protein kinase was partially purified from Streptomyces albus. When RNA polymerase was treated with protein kinase in vitro the activity of RNA polymerase was markedly enhanced. Furthermore, a protein of M = 65 kDa was isolated which, after being phosphorylated, stimulated RNA polymerase activity in vitro. Because neither the beta-subunits nor the alpha-subunits of RNA polymerase were phosphorylated it is assumed that phosphorylation of the 65 kDa protein may regulate the activity of RNA polymerase in streptomycetes.
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