Active Disruption of an RNA-protein Interaction by a DExH/D RNA Helicase

Science. 2001 Jan 5;291(5501):121-5. doi: 10.1126/science.291.5501.121.

Abstract

All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.

Publication types

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

MeSH terms

  • 3' Untranslated Regions / metabolism
  • Acid Anhydride Hydrolases / chemistry
  • Acid Anhydride Hydrolases / metabolism*
  • Adenosine Triphosphate / metabolism
  • Base Sequence
  • Binding Sites
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleoside-Triphosphatase
  • Protein Binding
  • Protein Conformation
  • RNA / chemistry
  • RNA / metabolism*
  • RNA Helicases / chemistry
  • RNA Helicases / metabolism*
  • RNA-Binding Proteins*
  • Ribonucleoprotein, U1 Small Nuclear / metabolism*

Substances

  • 3' Untranslated Regions
  • RNA-Binding Proteins
  • Ribonucleoprotein, U1 Small Nuclear
  • U1A protein
  • RNA
  • Adenosine Triphosphate
  • Acid Anhydride Hydrolases
  • Nucleoside-Triphosphatase
  • RNA Helicases