Ribonucleic acid release activity of transcription termination protein rho is dependent on the hydrolysis of nucleoside triphosphates.
Ribonucleic acid release activity of transcription termination protein rho is dependent on the hydrolysis of nucleoside triphosphates.
复制标题
转录终止蛋白rho的核糖核酸释放活性依赖于三磷酸核苷的水解。
DOI:
10.1021/bi00559a022
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发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
Conaway,R
中科院分区:
文献类型:
--
作者:
Richardson,JP;Conaway,R
John P. Richardson* and Ronald Conaway* abstract: An assay is devised to measure p-dependent release of RNA chains from transcription complexes. It is shown that p stimulates therelease of RNA fromisolated ternary tran-scription complexes consisting of nascent RNA molecules, Escherichia coli RNA polymerase, and T7 DNA and that this stimulation is dependent on the presence of a nucleotide substrate for p-NTPase. Several experiments lead to the conclusion that release is a direct consequence of a NTP hy-drolysis dependent p action on the RNA. First, the NTP requirement is satisfied by any of the nucleotides which are substrates for p-NTPase but is not satisfied by nucleotides that are not hydrolyzed by p action. Furthermore, the fact that some of the nucleotides that do activate release are poor substrates for RNA polymerase suggests that release is not dependent upon further nucleotide addition to the nascent chain. Second, the reaction conditions for release and RNA-I^. NA polymerase from Escherichia coli catalyzes the po-lymerization of RNA from a double-helical DNA template by a processive mechanism (Krakow et al., 1976). After initiation, an RNA chain is not released from its complex with the enzyme and the DNA until its synthesis is fully terminated. Since the rate of addition of nucleotides to a nascent RNA is not uniform at all sequences in the DNA (Darlix & Fro-mageot, 1972; Maizels, 1973; Rosenberg et al., 1978), there will be regions where RNA polymerase will pause