Protein kinase of bacteriophage T7 induces the phosphorylation of only a small number of proteins in the infected cell.
Protein kinase of bacteriophage T7 induces the phosphorylation of only a small number of proteins in the infected cell.
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噬菌体 T7 的蛋白激酶仅诱导受感染细胞中少量蛋白质的磷酸化。
DOI：
10.1016/0042-6822(90)90437-v
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发表时间：
1990
期刊：
影响因子：
3.7
通讯作者：
Allen W. Nicholson
中科院分区：
文献类型：
--
作者：
E. S. Robertson;Allen W. Nicholson
噬菌体T7表达由早期基因0.7编码的丝氨酸/苏氨酸特异性、cAMP非依赖性蛋白激酶活性。用一维SDS-聚丙烯酰胺凝胶电泳检测了T7感染的大肠杆菌中gp0.7蛋白激酶表达特异性产生的磷蛋白。只有七个主要的，稳定的磷蛋白依赖于gp0.7蛋白激酶的表达进行观察。先前已经鉴定了两种gp0.7蛋白激酶特异性磷蛋白：RNA聚合酶的β′亚基和RNA加工酶RNase III。在30 ℃感染后9-11分钟出现gp0.7催化的蛋白磷酸化活性。新的磷蛋白具有与未感染的细胞磷蛋白相当的代谢稳定性。T7蛋白激酶的表达引起大肠杆菌B、C或K菌株中相同的有限蛋白质组的磷酸化。杆菌T3和BA 14噬菌体蛋白激酶活性的表达也产生相同的磷蛋白。
Bacteriophage T7 expresses a serine/threonine-specific, cAMP-independent protein kinase activity encoded by the early gene 0.7. The phosphoproteins specifically resulting from gp0.7 protein kinase expression in T7-infectedEscherichia colihave been examined by one-dimensional, SDS-polyacrylamide gel electrophoresis. Only seven major, stable phosphoproteins dependent on gp0.7 protein kinase expression are observed. Two of the gp0.7 protein kinase-specific phosphoproteins observed have been previously identified: the β′ subunit of RNA polymerase and the RNA processing enzyme RNase III. The gp0.7-catalyzed protein phosphorylation activity appears at 9–11 min postinfection at 30°. The new phosphoproteins have a metabolic stability comparable to that of uninfected cell phosphoproteins. T7 protein kinase expression causes the phosphorylation of the same, limited set of proteins in B, C, or K strains ofE. coli. Expression of the T3 and BA 14 phage protein kinase activities also produces the same phosphoproteins.