杆状病毒DNA解旋酶P143的DNA与ATP结合活性
DNA and ATP binding activities of the baculovirus DNA helicase P143.
作者信息
McDougal V V, Guarino L A
机构信息
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128, USA.
出版信息
J Virol. 2001 Aug;75(15):7206-9. doi: 10.1128/JVI.75.15.7206-7209.2001.
Abstract
P143 is a DNA helicase that tightly binds both double-stranded and single-stranded DNA. DNA-protein complexes rapidly dissociated in the presence of ATP and Mg(2+). This finding suggests that ATP hydrolysis causes a conformational change in P143 which decreases affinity for DNA. This supports the model of an inchworm mechanism of DNA unwinding.
摘要
P143是一种DNA解旋酶，它能紧密结合双链和单链DNA。在ATP和Mg(2+)存在的情况下，DNA - 蛋白质复合物会迅速解离。这一发现表明，ATP水解会导致P143发生构象变化，从而降低其对DNA的亲和力。这支持了DNA解旋的尺蠖机制模型。
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本文引用的文献
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The Autographa californica nuclear polyhedrosis virus p143 gene encodes a DNA helicase.苜蓿银纹夜蛾核型多角体病毒p143基因编码一种DNA解旋酶。
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A baculovirus single-stranded DNA binding protein, LEF-3, mediates the nuclear localization of the putative helicase P143.杆状病毒单链DNA结合蛋白LEF-3介导假定解旋酶P143的核定位。
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