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Evidence for a mediator cycle at the initiation of transcription
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; and Imperial Cancer Research Fund Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; and Imperial Cancer Research Fund Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; and Imperial Cancer Research Fund Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; and Imperial Cancer Research Fund Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom.
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1997 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 94, no 12, p. 6075-6078Article in journal (Refereed) Published
Abstract [en]

Free and elongating (DNA-bound) forms of RNA polymerase II were separated from yeast. Most cellular polymerase II was found in the elongating fraction, which contained all enzyme phosphorylated on the C-terminal domain and none of the 15-subunit mediator of transcriptional regulation. These and other findings suggest that mediator enters and leaves initiation complexes during every round of transcription, in a process that may be coupled to C-terminal domain phosphorylation.

Place, publisher, year, edition, pages
Proceedings of the National Academy of Sciences (PNAS), 1997. Vol. 94, no 12, p. 6075-6078
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Molecular Biology
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URN: urn:nbn:se:umu:diva-236221DOI: 10.1073/pnas.94.12.6075ISI: A1997XD84400020PubMedID: 9177171Scopus ID: 2-s2.0-0030947346OAI: oai:DiVA.org:umu-236221DiVA, id: diva2:1943021
Available from: 2025-03-07 Created: 2025-03-07 Last updated: 2025-03-10Bibliographically approved

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