The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities

被引：118

作者：

Sedman, J ^{[1
]}

Stenlund, A ^{[1
]}

机构：

[1] Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA

来源：

JOURNAL OF VIROLOGY | 1998年 / 72卷 / 08期

关键词：

D O I：

10.1128/JVI.72.8.6893-6897.1998

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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,ve 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.

引用

页码：6893 / 6897

页数：5

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