Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication

Schuck, S., Stenlund, A. (August 2006) Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication. J Virol, 80 (15). pp. 7491-9. ISSN 0022-538X (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/16840329
DOI: 10.1128/jvi.00435-06

Abstract

The E1 protein from papillomaviruses is a multifunctional protein with complex functions required for the initiation of viral DNA replication. We have performed a surface mutagenesis of the well-characterized E1 DNA binding domain (DBD). We demonstrate that substitutions of multiple residues on the surface of the E1 DBD are defective for DNA replication without affecting the DNA binding activity of the protein. The defects of individual substitutions include failure to form the double trimer that melts the ori and failure to form the double hexamer that unwinds the ori. These results demonstrate that the DBD plays an essential role in multiple DNA replication-related processes apart from DNA binding.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Substitution Animals Binding Sites Bovine papillomavirus 1 genetics metabolism Cattle DNA Replication DNA Viral genetics metabolism DNA Binding Proteins genetics metabolism Gene Expression Regulation Viral Mutagenesis Protein Structure Tertiary Viral Proteins genetics metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
organism description > virus > papillomavirus
CSHL Authors:
Communities: CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date: August 2006
Date Deposited: 15 Mar 2012 14:15
Last Modified: 01 Mar 2013 16:43
PMCID: PMC1563737
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25178

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving