Comparative analysis of tertiary structure elements in signal recognition particle RNA

Christian Zwieb, Florian Müller, Niels Larsen

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


Background: The signal recognition particle (SRP) is a ribonucleoprotein complex that associates with ribosomes to promote co-translational translocation of proteins across biological membranes. We have used comparative analysis of a large number of bacterial, archaeal, and eukaryotic SRP RNA sequences to derive shared tertiary SRP RNA structure elements. Results: A representative three-dimensional model of the human SRP RNA is shown that includes single-stranded intrahelical and interhelical RNA loops and incorporates data from enzymatic and chemical modification, electron microscopy, and site-directed mutagenesis. Properties of the SRP RNA model are an overall extended dumbbell-shaped structure (260 Å × 70 Å) with a pseudoknot in the small SRP domain (a pairing of 12-UGGC-15 with 33-GCUA-36), and a tertiary interaction in the large SRP domain (198-GA-199 with 232-GU-233). Conclusions: The RNA 'knuckle' formed in helix 8 of SRP RNA appears to constitute the binding site for protein SRP54 or its bacterial equivalent, protein P48. A dynamic property of this feature may explain the hierarchical assembly of proteins SRP19 and SRP54 in the large SRP domain. Furthermore, the human SRP RNA model serves as a framework to understand details of the structure and function of SRP in all organisms and is presented to stimulate further experimentation in this area.

Original languageEnglish (US)
Pages (from-to)315-324
Number of pages10
JournalFolding and Design
Issue number4
StatePublished - 1996
Externally publishedYes


  • Comparative sequence analysis
  • Pseudoknot
  • RNA folding
  • RNA tetraloop
  • RNA-protein interactions
  • Tertiary interaction
  • Translation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


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