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PMID: 8551585 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cooperative assembly of EBNA1 on the Epstein-Barr virus latent origin of replication.

Journal of virology ·Vol. 70 ·No. 2 ·1996-02-00 ·Pages 1228-31

Summers H, Barwell JA, Pfuetzner RA, Edwards AM, Frappier L

Abstract

The EBNA1 protein of Epstein-Barr virus (EBV) activates DNA replication by binding to multiple copies of its 18-bp recognition sequence present in the Epstein-Barr virus latent origin of DNA replication, oriP. Using electrophoretic mobility shift assays, we have localized the minimal DNA binding domain of EBNA1 to between amino acids 470 and 607. We have also demonstrated that EBNA1 assembles cooperatively on the dyad symmetry subelement of oriP and that this cooperative interaction is mediated by residues within the minimal DNA binding and dimerization domain of EBNA1.

MeSH Terms
Antigens, Viral/genetics,metabolism Base Sequence Binding Sites DNA Primers DNA, Viral/metabolism DNA-Binding Proteins/genetics,metabolism Epstein-Barr Virus Nuclear Antigens Molecular Sequence Data Replication Origin Virus Assembly
Chemicals
Antigens, Viral DNA Primers DNA, Viral DNA-Binding Proteins Epstein-Barr Virus Nuclear Antigens
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Summers H
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
Barwell J A
Pfuetzner R A
Edwards A M
Frappier L
References (23)
23 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.70.2.1228-1231.1996
Published
1996-02-00
Pages
1228-31
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC189933
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.70.2.1228-1231.1996 PMC Full Text View journal details
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