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• W1932236103 abstract "Research Article15 June 1994free access Functional interaction between the HCMV IE2 transactivator and the retinoblastoma protein. C. Hagemeier C. Hagemeier Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author R. Caswell R. Caswell Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author G. Hayhurst G. Hayhurst Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author J. Sinclair J. Sinclair Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author T. Kouzarides T. Kouzarides Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author C. Hagemeier C. Hagemeier Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author R. Caswell R. Caswell Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author G. Hayhurst G. Hayhurst Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author J. Sinclair J. Sinclair Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author T. Kouzarides T. Kouzarides Wellcome/CRC Institute, Cambridge, UK. Search for more papers by this author Author Information C. Hagemeier1, R. Caswell1, G. Hayhurst1, J. Sinclair1 and T. Kouzarides1 1Wellcome/CRC Institute, Cambridge, UK. The EMBO Journal (1994)13:2897-2903https://doi.org/10.1002/j.1460-2075.1994.tb06584.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The 86 kDa immediate early IE2 protein of human cytomegalovirus (HCMV) can activate transcription of both viral and cellular genes and can repress transcription from its own promoter. Using two in vivo assays, we provide evidence of a functional interaction between IE2 and the retinoblastoma (RB) protein: IE2 alleviates RB-induced repression of a promoter bearing E2F binding sites and RB alleviates IE2-mediated repression of its own promoter. These functional effects are likely to be a result of a direct contact between IE2 and RB, which we can demonstrate both in vitro and in HCMV-infected cells. The interaction between IE2 and RB shows similar characteristics to the interaction between RB and E1A. First, binding to IE2 requires an intact RB pocket domain. Secondly, the binding is sensitive to the phosphorylation state of RB, because cyclin A-CDK-induced phosphorylation of RB diminishes IE2 binding. Thirdly, the IE2 domain required for RB binding is separate to the domains necessary for TBP and TFIIB binding. Our results demonstrate that large and small DNA viruses have a common interface with the host cell, namely the association with the RB tumour suppressor protein. Previous ArticleNext Article Volume 13Issue 121 June 1994In this issue RelatedDetailsLoading ..." @default.
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• W1932236103 title "Functional interaction between the HCMV IE2 transactivator and the retinoblastoma protein." @default.
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