乳头瘤病毒E1蛋白形成一种具有ATP酶和DNA解旋酶活性的DNA依赖性六聚体复合物。
The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities.
作者信息
Sedman J, Stenlund A
机构信息
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
出版信息
J Virol. 1998 Aug;72(8):6893-7. doi: 10.1128/JVI.72.8.6893-6897.1998.
Abstract
The E1 protein from bovine papillomavirus has site-specific DNA binding activity, DNA helicase activity, and DNA-dependent ATPase activity consistent with the properties of an initiator protein. Here we have identified and characterized a novel oligomeric form of E1 that is associated with the ATPase and DNA helicase activities and whose formation is strongly stimulated by single-stranded DNA. This oligomeric form corresponds to a hexamer of E1.
摘要
来自牛乳头瘤病毒的E1蛋白具有位点特异性DNA结合活性、DNA解旋酶活性和依赖于DNA的ATP酶活性，这些活性与引发蛋白的特性相符。在这里，我们鉴定并表征了一种新型的E1寡聚体形式，它与ATP酶和DNA解旋酶活性相关，并且其形成受到单链DNA的强烈刺激。这种寡聚体形式对应于E1的六聚体。
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