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

H Lu; L Zawel; L Fisher; J M Egly; D Reinberg

doi:10.1038/358641a0

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.

Authors

H Lu¹, L Zawel, L Fisher, J M Egly, D Reinberg

Affiliation

¹ Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854-5635.

PMID: 1495560
DOI: 10.1038/358641a0

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 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*

Substances

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