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Article: Epstein-Barr virus BamHI-A rightward transcript-encoded RPMS protein interacts with the CBF1-associated corepressor CIR to negatively regulate the activity of EBNA2 and NotchIC

TitleEpstein-Barr virus BamHI-A rightward transcript-encoded RPMS protein interacts with the CBF1-associated corepressor CIR to negatively regulate the activity of EBNA2 and NotchIC
Authors
Issue Date2001
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 2001, v. 75 n. 6, p. 2946-2956 How to Cite?
AbstractThe Epstein-Barr virus (EBV) BamHI-A rightward transcripts (BARTs) are expressed in all EBV-associated tumors as well as in latently infected B cells in vivo and cultured B-cell lines. One of the BART family transcripts contains an open reading frame, RPMS1, that encodes a nuclear protein termed RPMS. Reverse transcription-PCR analysis revealed that BART transcripts with the splicing pattern that generates the RPMS1 open reading frame are commonly expressed in EBV-positive lymphoblastoid cell lines and are also detected in Hodgkin's disease tissues. Experiments undertaken to determine the function of RPMS revealed that RPMS interacts with both CBF1 and components of the CBF1-associated corepressor complex. RPMS interaction with CBF1 was demonstrated in a glutathione S-transferase (GST) affinity assay and by the ability of RPMS to alter the intracellular localization of a mutant CBF1. A GaI4-RPMS fusion protein mediated transcriptional repression, suggesting an additional interaction between RPMS and corepressor proteins. GST affinity assays revealed interaction between RPMS and the corepressor Sin3A and CIR. The RPMS-CIR interaction was further substantiated in mammalian two-hybrid, coimmunoprecipitation, and colocalization experiments. RPMS has been shown to interfere with NotchIC and EBNA2 activation of CBF1-containing promoters in reporter assays. Consistent with this function, immunofluorescence assays performed on cotransfected cells showed that there was colocalization of RPMS with NotchIC and with EBNA2 in intranuclear punctate speckles. The effect of RPMS on NotchIC function was further examined in a muscle cell differentiation assay where RPMS was found to partially reverse NotchIC-mediated inhibition of differentiation. The mechanism of RPMS action was examined in cotransfection and mammalian two-hybrid assays. The results revealed that RPMS blocked relief of CBF1-mediated repression and interfered with SKIP-CIR interactions. We conclude that RPMS acts as a negative regulator of EBNA2 and Notch activity through its interactions with the CBF1-associated corepressor complex.
Persistent Identifierhttp://hdl.handle.net/10722/157329
ISSN
2015 Impact Factor: 4.606
2015 SCImago Journal Rankings: 3.347
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Jen_US
dc.contributor.authorChen, Hen_US
dc.contributor.authorWeinmaster, Gen_US
dc.contributor.authorHayward, SDen_US
dc.date.accessioned2012-08-08T08:48:57Z-
dc.date.available2012-08-08T08:48:57Z-
dc.date.issued2001en_US
dc.identifier.citationJournal Of Virology, 2001, v. 75 n. 6, p. 2946-2956en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/157329-
dc.description.abstractThe Epstein-Barr virus (EBV) BamHI-A rightward transcripts (BARTs) are expressed in all EBV-associated tumors as well as in latently infected B cells in vivo and cultured B-cell lines. One of the BART family transcripts contains an open reading frame, RPMS1, that encodes a nuclear protein termed RPMS. Reverse transcription-PCR analysis revealed that BART transcripts with the splicing pattern that generates the RPMS1 open reading frame are commonly expressed in EBV-positive lymphoblastoid cell lines and are also detected in Hodgkin's disease tissues. Experiments undertaken to determine the function of RPMS revealed that RPMS interacts with both CBF1 and components of the CBF1-associated corepressor complex. RPMS interaction with CBF1 was demonstrated in a glutathione S-transferase (GST) affinity assay and by the ability of RPMS to alter the intracellular localization of a mutant CBF1. A GaI4-RPMS fusion protein mediated transcriptional repression, suggesting an additional interaction between RPMS and corepressor proteins. GST affinity assays revealed interaction between RPMS and the corepressor Sin3A and CIR. The RPMS-CIR interaction was further substantiated in mammalian two-hybrid, coimmunoprecipitation, and colocalization experiments. RPMS has been shown to interfere with NotchIC and EBNA2 activation of CBF1-containing promoters in reporter assays. Consistent with this function, immunofluorescence assays performed on cotransfected cells showed that there was colocalization of RPMS with NotchIC and with EBNA2 in intranuclear punctate speckles. The effect of RPMS on NotchIC function was further examined in a muscle cell differentiation assay where RPMS was found to partially reverse NotchIC-mediated inhibition of differentiation. The mechanism of RPMS action was examined in cotransfection and mammalian two-hybrid assays. The results revealed that RPMS blocked relief of CBF1-mediated repression and interfered with SKIP-CIR interactions. We conclude that RPMS acts as a negative regulator of EBNA2 and Notch activity through its interactions with the CBF1-associated corepressor complex.en_US
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_US
dc.relation.ispartofJournal of Virologyen_US
dc.subject.meshCell Differentiationen_US
dc.subject.meshCell Lineen_US
dc.subject.meshDeoxyribonuclease Bamhi - Metabolismen_US
dc.subject.meshEpstein-Barr Virus Nuclear Antigens - Genetics - Metabolismen_US
dc.subject.meshGene Expression Regulation, Viralen_US
dc.subject.meshHerpesvirus 4, Human - Genetics - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Proteins - Genetics - Metabolismen_US
dc.subject.meshMuscles - Cytologyen_US
dc.subject.meshNeoplasm Proteinsen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshRna, Viral - Chemistry - Genetics - Metabolismen_US
dc.subject.meshReceptors, Notchen_US
dc.subject.meshRepressor Proteins - Genetics - Metabolismen_US
dc.subject.meshTranscription, Geneticen_US
dc.subject.meshTransfectionen_US
dc.subject.meshViral Proteinsen_US
dc.titleEpstein-Barr virus BamHI-A rightward transcript-encoded RPMS protein interacts with the CBF1-associated corepressor CIR to negatively regulate the activity of EBNA2 and NotchICen_US
dc.typeArticleen_US
dc.identifier.emailChen, H:hlchen@hkucc.hku.hken_US
dc.identifier.authorityChen, H=rp00383en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/JVI.75.6.2946-2956.2001en_US
dc.identifier.pmid11222720-
dc.identifier.scopuseid_2-s2.0-0035129844en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035129844&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume75en_US
dc.identifier.issue6en_US
dc.identifier.spage2946en_US
dc.identifier.epage2956en_US
dc.identifier.isiWOS:000167160400048-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhang, J=35202802400en_US
dc.identifier.scopusauthoridChen, H=26643315400en_US
dc.identifier.scopusauthoridWeinmaster, G=8777036700en_US
dc.identifier.scopusauthoridHayward, SD=7102776214en_US

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