Smardová J, Dobrová Z, Havránek M, Janecek J
Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.
Folia Microbiol (Praha). 1992;37(1):53-9. doi: 10.1007/BF02814581.
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.
从石榴链霉菌中分离出RNA聚合酶，并从白色链霉菌中部分纯化出蛋白激酶。当RNA聚合酶在体外与蛋白激酶一起处理时，RNA聚合酶的活性显著增强。此外，分离出一种分子量为65 kDa的蛋白质，该蛋白质在磷酸化后，在体外刺激RNA聚合酶活性。由于RNA聚合酶的β亚基和α亚基均未被磷酸化，因此推测65 kDa蛋白质的磷酸化可能调节链霉菌中RNA聚合酶的活性。
