The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins

Joachim Herz, Nicholas Flint, Keith Stanley, Rainer Frank, Bernhard Dobberstein

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

Original languageEnglish (US)
Pages (from-to)103-107
Number of pages5
JournalFEBS Letters
Volume276
Issue number1-2
DOIs
StatePublished - Dec 10 1990

Keywords

  • Glycine-rich
  • Ribonucleoprotein particle
  • Signal recognition particle
  • Translocation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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