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
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.