The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72

Elena Iakhiaeva, Jacek Wower, Iwona K. Wower, Christian Zwieb

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The signal recognition particle (SRP) plays a pivotal role in transporting proteins to cell membranes. In higher eukaryotes, SRP consists of an RNA molecule and six proteins. The largest of the SRP proteins, SRP72, was found previously to bind to the SRP RNA. A fragment of human SRP72 (72c′) bound effectively to human SRP RNA but only weakly to the similar SRP RNA of the archaeon Methanococcus jannaschii. Chimeras between the human and M. jannaschii SRP RNAs were constructed and used as substrates for 72c′. SRP RNA helical section 5e contained the 72c′ binding site. Systematic alteration within 5e revealed that the A240G and A240C changes dramatically reduced the binding of 72c′. Human SRP RNA with a single A240G change was unable to form a complex with full-length human SRP72. Two small RNA fragments, one composed of helical section 5ef, the other of section 5e, competed equally well for the binding of 72c′, demonstrating that no other regions of the SRPR RNA were required. The biochemical data completely agreed with the nucleotide conservation pattern observed across the phylogenetic spectrum. Thus, most eukaryotic SRP RNAs are likely to require for function an adenosine within their 5e motifs. The human 5ef RNA was remarkably resistant to ribonucleolytic attack suggesting that the 240-AUC-242 "loop" and its surrounding nucleotides form a peculiar compact structure recognized only by SRP72. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1143-1153
Number of pages11
JournalRNA
Volume14
Issue number6
DOIs
StatePublished - Jun 2008

Keywords

  • Protein-RNA interactions
  • RNP
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Molecular Biology

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