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A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.
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1994 (English)In: Cell, ISSN 0092-8674, E-ISSN 1097-4172, Vol. 77, no 4, 599-608 p.Article in journal (Refereed) Published
Abstract [en]

A mediator was isolated from yeast that enabled a response to the activator proteins GAL4-VP16 and GCN4 in a transcription system reconstituted with essentially homogeneous basal factors and RNA polymerase II. The mediator comprised some 20 polypeptides, including the three subunits of TFIIF and other polypeptides cross-reactive with antisera against GAL11, SUG1, SRB2, SRB4, SRB5, and SRB6 proteins. Mediator not only enabled activated transcription but also conferred 8-fold greater activity in basal transcription and 12-fold greater efficiency of phosphorylation of RNA polymerase II by the TFIIH-associated C-terminal repeat domain (CTD) kinase, indicative of mediator-CTD interaction. A holoenzyme form of RNA polymerase II was independently isolated that supported a response to activator proteins with purified basal factors. The holoenzyme proved to consist of mediator associated with core 12-subunit RNA polymerase II.

Place, publisher, year, edition, pages
1994. Vol. 77, no 4, 599-608 p.
URN: urn:nbn:se:umu:diva-42466PubMedID: 8187178OAI: diva2:409300
Available from: 2011-04-07 Created: 2011-04-07 Last updated: 2011-04-07

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Björklund, Stefan
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