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

Citation
Mr. Hicks et al., Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1, J VIROLOGY, 75(11), 2001, pp. 5381-5384
Citations number
31
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF VIROLOGY
ISSN journal
0022538X → ACNP
Volume
75
Issue
11
Year of publication
2001
Pages
5381 - 5384
Database
ISI
SICI code
0022-538X(200106)75:11<5381:BAONVO>2.0.ZU;2-H
Abstract
BZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replica tion. 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.