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

Sedman, J., Stenlund, A. (August 1998) The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities. J Virol, 72 (8). pp. 6893-7. ISSN 0022-538X (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/9658141

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.

Item Type: Paper
Uncontrolled Keywords: Adenosinetriphosphatase metabolism Animals Cattle DNA metabolism DNA Helicases metabolism DNA Single Stranded DNA Binding Proteins metabolism Papillomavirus Bovine metabolism Research Support US Govt PHS Viral Proteins metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > helicase
CSHL Authors:
Communities: CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date: August 1998
Date Deposited: 06 Mar 2012 17:51
Last Modified: 14 Feb 2017 20:24
PMCID: PMC109901
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25191

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