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PMID: 1495560 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Nature ·Vol. 358 ·No. 6388 ·1992-08-20 ·Pages 641-5

Lu H, Zawel L, Fisher L, Egly JM, Reinberg D

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.

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,ultrastructure Transcription, Genetic
Chemicals
Macromolecular Substances Transcription Factors Adenosine Triphosphate DNA Protein Kinases RNA Polymerase II
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lu H
Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854-5635.
Zawel L
Fisher L
Egly J M
Reinberg D
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-08-20
Pages
641-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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