Mutation of a single amino acid residue in the basic region of the Epstein-Barr virus (EBV) lytic cycle switch protein Zta (BZLF1) prevents reactivation of EBV from latency.
Zta, the product of the BZLF1 gene carried by Epstein-Barr virus (EBV), is crucial for reactivation of EBV from latency. Zta is a member of the bZIP family of transcription factors, and in common with many of these, Zta possesses a conserved cysteine residue in its basic region (C189) and a further cysteine residue in its ZIP region (C222). We demonstrate that C189 is required to reactivate EBV from latency but C222 is not and that this single amino acid affects two independent functions of Zta, (i) binding to a Zta-responsive site and (ii) manipulating the cell cycle.
Schelcher
Celine
C
School of Life Sciences, University of Sussex, Brighton BN1 9QG, United Kingdom.
Valencia
Sarah
S
Delecluse
Henri-Jacques
HJ
Hicks
Matthew
M
Sinclair
Alison J
AJ
D002453:Cell Cycle / Q000502:physiology; D002460:Cell Line; D003545:Cysteine / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D004854:Herpesvirus 4, Human / Q000502:physiology*; D006801:Humans; D009154:Mutation; D015534:Trans-Activators / Q000737:chemistry / Q000502:physiology*; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology*; D014775:Virus Activation
C063676:BZLF1 protein, Herpesvirus 4, Human; D004268:DNA-Binding Proteins; D015534:Trans-Activators; D014764:Viral Proteins; D003545:Cysteine