由大肠杆菌UvrABC核酸内切酶催化的切割反应过程中形成的蛋白质复合物。
Protein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease.
作者信息
Yeung A T, Mattes W B, Grossman L
出版信息
Nucleic Acids Res. 1986 Mar 25;14(6):2567-82. doi: 10.1093/nar/14.6.2567.
Abstract
An examination has been made into the nature of the nucleoprotein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease when acting on a pyrimidine dimer-containing fd RF-I DNA species. The complexes of proteins and DNA form in unique stages. The first stage of binding involves an ATP-stimulated interaction of the UvrA protein with duplex DNA containing pyrimidine dimer sites. The UvrB protein significantly stabilizes the UvrA-pyrimidine dimer containing DNA complex which, in turn, provides a foundation for the binding of UvrC to activate the UvrABC endonuclease. The binding of one molecule of UvrC to each UvrAB-damaged DNA complex is needed to catalyze incision in the vicinity of pyrimidine dimer sites. The UvrABC-DNA complex persists after the incision event suggesting that the lack of UvrABC turnover may be linked to other activities in the excision-repair pathway beyond the initial incision reaction.
摘要
对大肠杆菌UvrABC核酸内切酶催化切口反应过程中形成的核蛋白复合物的性质进行了研究，该反应作用于含嘧啶二聚体的fd RF-I DNA分子。蛋白质与DNA的复合物在独特阶段形成。结合的第一阶段涉及UvrA蛋白与含嘧啶二聚体位点的双链DNA的ATP刺激相互作用。UvrB蛋白显著稳定了含UvrA - 嘧啶二聚体的DNA复合物，进而为UvrC的结合提供基础以激活UvrABC核酸内切酶。每个UvrAB损伤的DNA复合物需要结合一分子UvrC来催化嘧啶二聚体位点附近的切口。切口事件后UvrABC - DNA复合物持续存在，这表明UvrABC周转的缺乏可能与切除修复途径中初始切口反应之外的其他活动有关。
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