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

Hicks, Matthew R., Balesaria, Sara, Medina-Palazon, Cahora, Pandya, Maya J., Woolfson, Derek N. and Sinclair, Alison J. (2001) Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1. Journal of Virology, 75 (11). pp. 5381-5384. ISSN 0022-538X

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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.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Alison Sinclair
Date Deposited: 06 Feb 2012 18:45
Last Modified: 02 May 2012 14:50
URI: http://sro.sussex.ac.uk/id/eprint/18156
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