RNA Helicase A Mediates Association of CBP With RNA Polymerase II

Cell. 1997 Sep 19;90(6):1107-12. doi: 10.1016/s0092-8674(00)80376-1.

Abstract

The coactivator CBP has been proposed to stimulate the expression of certain signal-dependent genes via its association with RNA polymerase II complexes. Here we show that complex formation between CBP and RNA polymerase II requires RNA helicase A (RHA), a nuclear DNA/RNA helicase that is related to the Drosophila male dosage compensation factor mle. In transient transfection assays, RHA was found to cooperate with CBP in mediating target gene activation via the CAMP responsive factor CREB. As a mutation in RHA that compromised its helicase activity correspondingly reduced CREB-dependent transcription, we propose that RHA may induce local changes in chromatin structure that promote engagement of the transcriptional apparatus on signal responsive promoters.

Publication types

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

MeSH terms

  • Animals
  • Cells, Cultured
  • Cyclic AMP Response Element-Binding Protein / analysis
  • Cyclic AMP Response Element-Binding Protein / metabolism*
  • DNA, Complementary / metabolism
  • Drosophila
  • Gene Expression Regulation, Enzymologic / physiology
  • Humans
  • Male
  • Phosphoserine
  • Precipitin Tests
  • Protein Binding / physiology
  • RNA Helicases
  • RNA Nucleotidyltransferases / metabolism*
  • RNA Polymerase II / analysis
  • RNA Polymerase II / metabolism*
  • Transcription, Genetic / physiology
  • Transcriptional Activation
  • Zinc Fingers / physiology

Substances

  • Cyclic AMP Response Element-Binding Protein
  • DNA, Complementary
  • Phosphoserine
  • RNA Nucleotidyltransferases
  • RNA Polymerase II
  • RNA Helicases