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

Nature. 1992 Aug 20;358(6388):641-5. doi: 10.1038/358641a0.


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 IIE, which is required for the stable association of TFIIH with the preinitiation complex, affects the processivity of TFIIH kinase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Cytoplasm / metabolism
  • DNA / metabolism
  • Gene Expression Regulation
  • Humans
  • In Vitro Techniques
  • Macromolecular Substances
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases / metabolism*
  • RNA Polymerase II / metabolism*
  • Transcription Factors / metabolism*
  • Transcription Factors / ultrastructure
  • Transcription, Genetic*


  • Macromolecular Substances
  • Transcription Factors
  • Adenosine Triphosphate
  • DNA
  • Protein Kinases
  • RNA Polymerase II