Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1.
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.
Hicks
M R
MR
School of Biological Sciences, School of Biological Sciences, University of Sussex, Brighton, East Sussex BN1 9QG, United Kingdom.
Balesaria
S
S
Medina-Palazon
C
C
Pandya
M J
MJ
Woolfson
D N
DN
Sinclair
A J
AJ
D000595:Amino Acid Sequence; D001402:B-Lymphocytes; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D020031:Epstein-Barr Virus Infections / Q000821:virology*; D014644:Genetic Variation; D004854:Herpesvirus 4, Human / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis / Q000138:chemical synthesis / Q000235:genetics; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics; D014407:Tumor Cells, Cultured; D014764:Viral Proteins
C063676:BZLF1 protein, Herpesvirus 4, Human; D004268:DNA-Binding Proteins; D010455:Peptides; D015534:Trans-Activators; D014764:Viral Proteins