Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation

Nature. 1994 Mar 10;368(6467):160-3. doi: 10.1038/368160a0.

Abstract

The general transcription factor TFIIE, together with other general transcription factors, is essential for transcription initiation by RNA polymerase II. TFIIE stimulates the TFIIH-dependent kinase activity that phosphorylates the carboxy-terminal domain of the largest subunit of RNA polymerase II, and possesses a helicase activity. Here we show that human TFIIH has DNA-dependent ATPase activity and we characterize the stimulatory effect of TFIIE on both the ATPase and kinase activities. We demonstrate that extensive phosphorylation of RNA polymerase II occurs in a TFIIE-dependent manner in both the absence and presence of DNA but, in the latter case, only at a late stage of preinitiation complex assembly. We also show that TFIIH specifically phosphorylates three general transcription factors, human TFIID tau (TBP), TFIIE-alpha and TFIIF-alpha (RAP74).

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • DNA Helicases*
  • DNA-Directed RNA Polymerases / metabolism
  • HeLa Cells
  • Humans
  • Mice
  • Molecular Sequence Data
  • Oligopeptides / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism
  • Rats
  • Transcription Factor TFIIH
  • Transcription Factors / metabolism*
  • Transcription Factors, TFII*
  • Transcription, Genetic*

Substances

  • Oligopeptides
  • Transcription Factors
  • Transcription Factors, TFII
  • transcription factor TFIIE
  • tyrosyl-seryl-prolyl-threonyl-seryl-prolyl-seryl-tyrosine
  • Transcription Factor TFIIH
  • Protein Kinases
  • carboxy-terminal domain kinase
  • DNA-Directed RNA Polymerases
  • Adenosine Triphosphatases
  • DNA Helicases