| pubmed-article:8709224 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0292369 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0812273 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:8709224 | lifeskim:mentions | umls-concept:C0949374 | lld:lifeskim |
| pubmed-article:8709224 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8709224 | pubmed:dateCreated | 1996-9-10 | lld:pubmed |
| pubmed-article:8709224 | pubmed:abstractText | Epstein-Barr nuclear antigen 2 (EBNA2), one of the six viral nuclear proteins expressed in latently infected B lymphocytes, is essential to the immortalization of B cells by Epstein-Barr virus (EBV). EBNA2 promotes transcriptional transactivation of viral and cellular genes by acting as an adapter molecule that binds to cellular sequence-specific DNA-binding proteins, JK recombination signal-binding protein (RBP-JK), and PU.1 and engages multiple members of the RNA polymerase II transcription complex. In the present study, we show that EBNA2 also interacts with hSNF5/Ini1, the human homolog of the yeast transcription factor SNF5. Gel filtration fractionation of partially purified EBV-positive lymphocyte nuclear extracts shows that a fraction of EBNA2 coelutes with both hSNF5/Ini1 and BRG1, a human homolog of SWI/SNF2, in the high-molecular-mass region (1.5 to 2.0 MDa) of a Superose 6 chromatogram. An affinity-purified rabbit antibody directed against hSNF5/Ini1 coimmunoprecipitates EBNA2 from this high-molecular-mass nuclear protein fraction, demonstrating that EBNA2 and hSNF5/Ini1 interact in vivo. This interaction is restricted to a subpopulation of phosphorylated viral EBNA2. Deletion mutation analysis of EBNA2 shows that the proline-rich aminoterminal end and a domain within the divergent region of EBNA2 mediate EBNA2-hSNF5/Ini1 interaction. Since the SNF-SWI complex participates in gene regulation through the alteration of nucleosome configuration and may be a component of the RNA polymerase II holoenzyme, the EBNA2-hSNF5/Ini1 interaction supports the hypothesis that EBNA2 facilitates transcriptional transactivation by acting as a transcription adapter molecule. We postulate that EBNA2 engages the hSNF-SWI complex to generate an open chromatin conformation at the EBNA2-responsive target genes, thereby potentiating the function of the RBP-JK-EBNA2-polymerase II transcription complex. | lld:pubmed |
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| pubmed-article:8709224 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8709224 | pubmed:citationSubset | IM | lld:pubmed |
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