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PMID: 11333921 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1.

Journal of virology ·Vol. 75 ·No. 11 ·2001-06-00 ·Pages 5381-4

Hicks MR, Balesaria S, Medina-Palazon C, Pandya MJ, Woolfson DN, Sinclair AJ

Abstract

BZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replication. On the basis of limited sequence homology and mutagenesis experiments, BZLF1 has been described as a member of the bZip family of transcription factors, but this prospect has not been rigorously tested to date. Here, we present biophysical analysis of the multimerization domain of BZLF1, from three natural variants of EBV, and demonstrate for the first time that the region between amino acids 196 and 227 is sufficient to direct folding as a coiled-coil dimer in vitro.

MeSH Terms
Amino Acid Sequence B-Lymphocytes Cell Line DNA-Binding Proteins/chemistry,genetics Epstein-Barr Virus Infections/virology Genetic Variation Herpesvirus 4, Human/chemistry,genetics Humans Molecular Sequence Data Peptides/analysis,chemical synthesis,genetics Spectrophotometry, Ultraviolet Temperature Trans-Activators/chemistry,genetics Tumor Cells, Cultured Viral Proteins
Chemicals
BZLF1 protein, Herpesvirus 4, Human DNA-Binding Proteins Peptides Trans-Activators Viral Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hicks M R
School of Biological Sciences, School of Biological Sciences, University of Sussex, Brighton, East Sussex BN1 9QG, United Kingdom.
Balesaria S
Medina-Palazon C
Pandya M J
Woolfson D N
Sinclair A J
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.75.11.5381-5384.2001
Published
2001-06-00
Pages
5381-4
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC114945
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.75.11.5381-5384.2001 PMC Full Text View journal details
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