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一种来自小麦胚芽的蛋白激酶，可使RNA聚合酶II的最大亚基磷酸化。

A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II.

作者信息

Guilfoyle T J

机构信息

Department of Biochemistry, University of Missouri, Columbia, 65211.

出版信息

Plant Cell. 1989 Aug;1(8):827-36. doi: 10.1105/tpc.1.8.827.

DOI:10.1105/tpc.1.8.827
PMID:2535525
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC159820/
Abstract

A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase IIA has been partially purified and characterized. The kinase has a native molecular weight of about 200 kilodaltons. This kinase utilizes Mg2+ and ATP and transfers about 20 phosphates to the heptapeptide repeats Pro-Thr-Ser-Pro-Ser-Tyr-Ser in the carboxyl-terminal domain of the 220-kilodalton subunit of soybean RNA polymerase II. This phosphorylation results in a mobility shift of the 220-kilodalton subunits of a variety of eukaryotic RNA polymerases to polypeptides ranging in size from greater than 220 kilodaltons to 240 kilodaltons on sodium dodecyl sulfate-polyacrylamide gels. The phosphorylation is highly specific to the heptapeptide repeats since a degraded subunit polypeptide of 180 kilodaltons that lacks the heptapeptide repeats is poorly phosphorylated. Synthetic heptapeptide repeat multimers inhibit the phosphorylation of the 220-kilodalton subunit.

摘要

从小麦胚芽中分离得到一种能使RNA聚合酶IIA最大亚基磷酸化的蛋白激酶，并对其进行了部分纯化和特性鉴定。该激酶的天然分子量约为200千道尔顿。此激酶利用Mg2+和ATP，并将约20个磷酸基团转移至大豆RNA聚合酶II 220千道尔顿亚基羧基末端结构域中的七肽重复序列Pro-Thr-Ser-Pro-Ser-Tyr-Ser上。这种磷酸化作用导致多种真核生物RNA聚合酶的220千道尔顿亚基在十二烷基硫酸钠-聚丙烯酰胺凝胶上的迁移率发生变化，变为大小从大于220千道尔顿到240千道尔顿不等的多肽。由于缺乏七肽重复序列的180千道尔顿降解亚基多肽磷酸化程度较低，所以这种磷酸化作用对七肽重复序列具有高度特异性。合成的七肽重复多聚体可抑制220千道尔顿亚基的磷酸化。

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