YidC and Oxa1 form dimeric insertion pores on the translating ribosome.
- Kohler R Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
- Boehringer D
- Greber B
- Bingel-Erlenmeyer R
- Collinson I
- Schaffitzel C
- Ban N
- 2009-05-20
Published in:
- Molecular cell. - 2009
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
SEC Translocation Channels
English
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.
- Language
-
- English
- Open access status
- green
- Identifiers
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- DOI 10.1016/j.molcel.2009.04.019
- PMID 19450532
- Persistent URL
- https://sonar.ch/global/documents/164287
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