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

التفاصيل البيبلوغرافية
العنوان: Coactivators p300 and PCAF physically and functionally interact with the foamy viral trans-activator
المؤلفون: Helmut, Bannert, Walter, Muranyi, Vasily V, Ogryzko, Yoshihiro, Nakatani, Rolf M, Flügel
المصدر: BMC Molecular Biology, Vol 5, Iss 1, p 16 (2004)
BMC Molecular Biology
بيانات النشر: BMC, 2004.
سنة النشر: 2004
مصطلحات موضوعية: Transcriptional Activation, animal structures, lcsh:QH426-470, Retroviridae Proteins, Cell Cycle Proteins, Kidney, Response Elements, Cell Line, Acetyltransferases, Cell Line, Tumor, Protein Interaction Mapping, Humans, p300-CBP Transcription Factors, lcsh:QH573-671, Histone Acetyltransferases, lcsh:Cytology, Nuclear Proteins, Protein Structure, Tertiary, DNA-Binding Proteins, lcsh:Genetics, Mutation, Trans-Activators, Spumavirus, Peptides, HeLa Cells, Transcription Factors, Research Article
الوصف: Background 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. Results 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. Conclusions Our data identify p300 and PCAF as functional partner molecules that directly interact with Bel1/Tas. Since the acetylation activities of the three coactivators reside in or bind to the C-terminal regions of p300, a C/H1 expression plasmid was used as inhibitor. This is the first report of a C/H1 domain-interacting retroviral trans-activator capable of partially blocking the strong Bel1/Tas-mediated activation of the C-terminal region of coactivator p300. The potential mechanisms and functional roles of the three histone and factor acetyltransferases p300, PCAF, and SRC-1 in Bel1/Tas-mediated trans-activation are discussed.
اللغة: English
تدمد: 1471-2199
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::778427e4ba44211a54df5b2149bd6734Test
http://www.biomedcentral.com/1471-2199/5/16Test
حقوق: OPEN
رقم الانضمام: edsair.pmid.dedup....778427e4ba44211a54df5b2149bd6734
قاعدة البيانات: OpenAIRE