YidC and Oxa1 form dimeric insertion pores on the translating ribosome

Rebecca Kohler, Daniel Boehringer, Basil Greber, Rouven Bingel-Erlenmeyer, Ian Collinson, Christiane Schaffitzel, Nenad Ban

Research output: Contribution to journalArticle (Academic Journal)peer-review

93 Citations (Scopus)

Abstract

The YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we present the structures of both Escherichia coli YidC and Saccharomyces cerevisiae Oxa1 bound to E. coli ribosome nascent chain complexes determined by cryo-electron microscopy. Dimers of YidC and Oxa1 are localized above the exit of the ribosomal tunnel. Crosslinking experiments show that the ribosome specifically stabilizes the dimeric state. Functionally important and conserved transmembrane helices of YidC and Oxa1 were localized at the dimer interface by cysteine crosslinking. Both Oxa1 and YidC dimers contact the ribosome at ribosomal protein L23 and conserved rRNA helices 59 and 24, similarly to what was observed for the nonhomologous SecYEG translocon. We suggest that dimers of the YidC and Oxa1 proteins form insertion pores and share a common overall architecture with the SecY monomer.

Original languageEnglish
Pages (from-to)344 - 353
Number of pages10
JournalMolecular Cell
Volume34
Issue number3
DOIs
Publication statusPublished - 15 May 2009

Bibliographical note

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Keywords

  • Bacterial Proteins
  • Cysteine
  • Dimerization
  • Electron Transport Complex IV
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Mitochondrial Proteins
  • Models, Molecular
  • Multiprotein Complexes
  • Nuclear Proteins
  • Oxidation-Reduction
  • Protein Binding
  • Protein Biosynthesis
  • Protein Structure, Quaternary
  • Ribosomes

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