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Cell Rep. 2017 Dec 26;21(13):3708-3716. doi: 10.1016/j.celrep.2017.12.006.

Identification of Oxa1 Homologs Operating in the Eukaryotic Endoplasmic Reticulum.

Author information

1
Department of Biochemistry and Molecular Biology , The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA; Cell and Molecular Biology Graduate Program , The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA.
2
Department of Biochemistry and Molecular Biology , The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA.
3
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
4
Department of Biochemistry and Molecular Biology , The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA. Electronic address: bkeenan@uchicago.edu.

Abstract

Members of the evolutionarily conserved Oxa1/Alb3/YidC family mediate membrane protein biogenesis at the mitochondrial inner membrane, chloroplast thylakoid membrane, and bacterial plasma membrane, respectively. Despite their broad phylogenetic distribution, no Oxa1/Alb3/YidC homologs are known to operate in eukaryotic cells outside the endosymbiotic organelles. Here, we present bioinformatic evidence that the tail-anchored protein insertion factor WRB/Get1, the "endoplasmic reticulum (ER) membrane complex" subunit EMC3, and TMCO1 are ER-resident homologs of the Oxa1/Alb3/YidC family. Topology mapping and co-evolution-based modeling demonstrate that Get1, EMC3, and TMCO1 share a conserved Oxa1-like architecture. Biochemical analysis of human TMCO1, the only homolog not previously linked to membrane protein biogenesis, shows that it associates with the Sec translocon and ribosomes. These findings suggest a specific biochemical function for TMCO1 and define a superfamily of proteins-the "Oxa1 superfamily"-whose shared function is to facilitate membrane protein biogenesis.

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