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Nature 358, 641-645 (20 August 1992) | doi:10.1038/358641a0; Accepted 15 July 1992

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

Hua Lu*, Leigh Zawel*, Laurent Fisher†, Jean-Marc Egly† & Danny Reinberg*‡

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