Effect of protein phosphorylation on the activity of RNA polymerase in streptomycetes.
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.
Smardová
J
J
Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.
Dobrová
Z
Z
Havránek
M
M
Janecek
J
J
D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000502:physiology*; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D014158:Transcription, Genetic / Q000502:physiology
D011494:Protein Kinases; D012321:DNA-Directed RNA Polymerases