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Sökning: onr:"swepub:oai:gup.ub.gu.se/51262" > Role of a consensus...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004099naa a2200313 4500
001oai:gup.ub.gu.se/51262
003SwePub
008240528s2007 | |||||||||||000 ||eng|
024a https://gup.ub.gu.se/publication/512622 URI
024a https://doi.org/10.1007/s11262-007-0116-x2 DOI
040 a (SwePub)gu
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Jansson, Ann,d 1950u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine4 aut0 (Swepub:gu)xjaann
2451 0a Role of a consensus AP-2 regulatory sequence within the Epstein-Barr Virus LMP1 promoter in EBNA2 mediated transactivation
264 c 2007-10-01
264 1b Springer Science and Business Media LLC,c 2007
520 a The Epstein-Barr virus (EBV) tumor-associated latent membrane protein 1 (LMP1) gene expression is transactivated by EBV nuclear antigen 2 (EBNA2) in human B cells. We previously reported that an E-box element at the LMP1 regulatory sequence (LRS) represses transcription of the LMP1 gene through the recruitment of a Max-Mad1-mSin3A complex. In the present study, using deletion/mutation analysis, and electrophoretic mobility shift assays, we show that the promoter region adjacent to the E-box (-59/-67) is required for the full repression conferred by E-box binding proteins. The repressive effect of these factors was overcome by an inhibitor of histone deacetylation, Trichostatin A (TSA), concurring with the reports that histone deacetylation plays an important role in repression mediated by Max-Mad1-mSin3A complex. Furthermore, ChIP analyses showed that histones at the transcriptionally active LMP1 promoter were hyperacetylated, whereas in the absence of transcription they were hypoacetylated. EBNA2 activation of the promoter required a consensus AP-2 sequence in the -103/-95 LRS region. While EMSA results and the low level of AP-2 factors expression in B cells argue against known AP-2 factors binding to this site, several pieces of evidence point to a similar mechanism of promoter activation as seen by AP-2 factors. We conclude that an AP-2 site-binding factor and EBNA2 act in concert to overcome the repression of the LMP1 promoter via the consensus AP-2 site. This activation showed strong correlation with histone hyperacetylation at the promoter, indicating this to be a major mechanism for the EBNA2 mediated LMP1 transactivation.
700a Johansson, Pegah,d 1978u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine4 aut0 (Swepub:gu)xjopeg
700a Yang, Weiwen,d 1967u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology4 aut0 (Swepub:gu)xyanwe
700a Palmqvist, Lars,d 1965u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine4 aut0 (Swepub:gu)xpalla
700a Sjöblom-Hallén, Anna,d 19654 aut
700a Rymo, Lars,d 1940u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine4 aut0 (Swepub:gu)xrymla
710a Göteborgs universitetb Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin4 org
773t Virus Genesd : Springer Science and Business Media LLCg 35:2, s. 203-14q 35:2<203-14x 0920-8569x 1572-994X
8564 8u https://gup.ub.gu.se/publication/51262
8564 8u https://doi.org/10.1007/s11262-007-0116-x

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