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.

Institute of Microbiology Czechoslovak Academy of Sciences Prague

Zobrazit více v PubMed

Nature. 1970 Aug 15;227(5259):680-5 PubMed

J Biochem. 1987 Feb;101(2):465-75 PubMed

J Mol Biol. 1974 Aug 25;87(4):685-96 PubMed

Arch Biochem Biophys. 1979 Nov;198(1):195-204 PubMed

Arch Biochem Biophys. 1977 Aug;182(2):404-8 PubMed

Biochemistry. 1975 Oct 21;14(21):4634-8 PubMed

Nucleic Acids Res. 1981 Jul 10;9(13):3129-38 PubMed

Chem Pharm Bull (Tokyo). 1987 Oct;35(10):4181-7 PubMed

Proc Natl Acad Sci U S A. 1975 Jul;72(7):2506-10 PubMed

J Virol. 1985 Jul;55(1):238-41 PubMed

Anal Biochem. 1976 May 7;72:248-54 PubMed

FEMS Microbiol Lett. 1990 Sep 1;59(1-2):145-8 PubMed

J Biol Chem. 1987 Sep 15;262(26):12468-74 PubMed

Isolation of DNA-dependent RNA polymerase from the thermophilic actinomycete Thermomonospora curvata