Protein-RNA recognition

Annu Rev Biochem. 1995;64:593-620. doi: 10.1146/annurev.bi.64.070195.003113.

Abstract

Specific interactions between RNAs and proteins are fundamental to many cellular processes, including the assembly and function of ribonucleoprotein particles (RNPs), such as ribosomes and spliceosomes and the post-transcriptional regulation of gene expression. Among the complexes studied to date are small RNAs bound to individual amino acids, tRNAs and tRNA fragments bound to their cognate aminoacyl-tRNA synthetases, and a variety of proteins bound to RNA single strands, hairpins, irregular helices, and tertiary structures stabilized by bound cations. Several proteins use a beta-sheet surface to bind RNAs, and others insert an alpha-helix into the widened major groove of a non-canonical RNA helix. Distortion or rearrangement of the RNA structure by bound protein is a common theme. The structural details of protein-RNA complexes are being resolved by nuclear magnetic resonance (NMR) and X-ray crystallography, but thorough thermodynamic analyses of recognition mechanisms have yet to be performed.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / metabolism
  • Amino Acyl-tRNA Synthetases / metabolism
  • Animals
  • Base Sequence
  • DNA / metabolism
  • Humans
  • Molecular Sequence Data
  • Molecular Structure
  • Peptides / metabolism
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism*
  • RNA / chemistry
  • RNA / genetics
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Ribonucleoproteins / metabolism
  • Zinc Fingers / genetics

Substances

  • Amino Acids
  • Peptides
  • Proteins
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • RNA
  • DNA
  • Amino Acyl-tRNA Synthetases