Coactivators p300 and PCAF physically and functionally interact with the foamy viral trans-activator

BMC Molecular Biology
Helmut BannertR M Flügel

Abstract

Foamy virus Bel1/Tas trans-activators act as key regulators of gene expression and directly bind to Bel1 response elements (BRE) in both the internal and the 5'LTR promoters leading to strong transcriptional trans-activation. Cellular coactivators interacting with Bel1/Tas are unknown to date. Transient expression assays, co-immunoprecipitation experiments, pull-down assays, and Western blot analysis were used to demonstrate that the coactivator p300 and histone acetyltransferase PCAF specifically interact with the retroviral trans-activator Bel1/Tas in vivo. Here we show that the Bel1/Tas-mediated trans-activation was enhanced by the coactivator p300, histone acetyltransferases PCAF and SRC-1 based on the crucial internal promoter BRE. The Bel1/Tas-interacting region was mapped to the C/H1 domain of p300 by co-immunoprecipitation and pull-down assays. In contrast, coactivator SRC-1 previously reported to bind to the C-terminal domain of p300 did not directly interact with the Bel1 protein but nevertheless enhanced Bel1/Tas-mediated trans-activation. Cotransfection of Bel1/Tas and p300C with an expression plasmid containing the C/H1domain partially inhibited the p300C-driven trans-activation. Our data identify p300 and PCAF as ...Continue Reading

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Citations

Sep 13, 2011·Journal of Biomolecular Screening·Peter T RyeWilliam A Lamarr
Nov 27, 2019·Viruses·Magdalena Materniak-KornasMartin Löchelt

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Methods Mentioned

BETA
acetylation
ubiquitination
sumoylation
transfection
immunoprecipitation
co-immunoprecipitation
co-immunoprecipitations
immunoprecipitations
pull-down
of

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