Nucleic Acids Research, 1995, Vol. 23, No. 10 1729-1736
© 1995
MOLECULAR BIOLOGY |
Physical and functional interaction of the Epstein-Barr virus BZLF1 transactivator with the retinoic acid receptors RAR
and RXR
1109 UNC-Lineberger Comprehensive Cancer Center USA 2Department of Medicine USA 3Department of Microbiology, University of North Carolina at Chapel Hill Chapel Hill, NC 27599-7295, USA
* To whom correspondence should be addressed
Received February 6, 1995. Accepted February 23, 1995.
Epstein-Barr virus (EBV) reactivation, indicated by induction of EBV early antigens from latently Infected lymphoid cell lines by phorbol esters, Is inhibited by retinoic acid (RA). Viral reactivation, which Is triggered by the immediate-early BZLF-1 (Z) viral gene product, is repressed by retinoic acid receptors (RARs) RAR
and RXR. These proteins negatively regulate Z-mediated transactlvation of the promoter for an EBV early gene product, early antigen-diffuse (EaD). Here we confirm a direct physical interaction between the AP1-llke protein Z and RXR and map the domains of Interaction In the Z protein and RXR. The domain required for homodimerlzation of Z is separate from that required for its interaction with RXR. Z also has the effect of repressing activation of an RAR-respon-slve cellular promoter (BRE). Point mutants In the dimerlzation domain of Z unable to interact with RXR do not repress RXR-medlated transactivation of BRE, the promoter for RARß, which suggests that Interaction between the two proteins is required for this repressor effect. The domain of RXR required for interaction with Z has been mapped, and is again separate from that required for homodimerization. These results indicate that a ‘cross-coupling’ or direct interaction between Z and RAR and RXR can modulate the reactivation of latent EBV infection and suggest that, reciprocally, the viral protein Z may influence cellular regulatory pathways.
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