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Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II

Nature volume 358, pages 641–645 (1992)Cite this article

Abstract

Phosphorylation of the carboxy-terminal domain of the largest subunit of RNA polymerase II is believed to control the transition from transcription initiation to elongation. The general transcription factor IIH (TFIIH) contains a kinase activity capable of phosphorylating this domain. Factors that promote the association of RNA polymerase II with the preinitiation complex stimulate this activity. The transcription factor HE, which is required for the stable association of TFIIH with the preinitiation complex, affects the processivity of TFIIH kinase.

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Authors and Affiliations

  1. Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 675 Hoes Lane, Piscataway, New Jersey, 08854–5635, USA

    Hua Lu, Leigh Zawel & Danny Reinberg

  2. Laboratoire de Genetique Moleculaire (CNRS), U184 (INSERM) des Eucaryotes, Faculte de Medecine, 67085, Strasbourg, France

    Laurent Fisher & Jean-Marc Egly

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  1. Hua Lu
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  2. Leigh Zawel
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  4. Jean-Marc Egly
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Lu, H., Zawel, L., Fisher, L. et al. Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature 358, 641–645 (1992). https://doi.org/10.1038/358641a0

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