Structural insights into the signal recognition particle

Annu Rev Biochem. 2004;73:539-57. doi: 10.1146/annurev.biochem.73.011303.074048.

Abstract

The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway.

Publication types

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

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Guanosine Triphosphate / metabolism
  • Models, Biological
  • Models, Molecular
  • Molecular Structure
  • Phylogeny
  • Protein Biosynthesis
  • Protein Conformation
  • Receptors, Cytoplasmic and Nuclear / chemistry
  • Receptors, Cytoplasmic and Nuclear / genetics
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Ribosomes / metabolism
  • Signal Recognition Particle / chemistry*
  • Signal Recognition Particle / genetics
  • Signal Recognition Particle / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Ffh protein, E coli
  • FtsY protein, Bacteria
  • Receptors, Cytoplasmic and Nuclear
  • Signal Recognition Particle
  • Guanosine Triphosphate