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Saccharomyces cerevisiae Cox18 complements the essential Sec‐independent function of Escherichia coli YidC
Author(s) -
van Bloois Edwin,
Koningstein Gregory,
Bauerschmitt Heike,
Herrmann Johannes M.,
Luirink Joen
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06094.x
Subject(s) - biogenesis , complementation , biology , inner membrane , protein targeting , escherichia coli , translocon , membrane protein , microbiology and biotechnology , saccharomyces cerevisiae , mitochondrion , signal recognition particle , bacterial outer membrane , biochemistry , yeast , membrane , ribosome , gene , phenotype , rna
Members of the YidC/Oxa1/Alb3 protein family function in the biogenesis of membrane proteins in bacteria, mitochondria and chloroplasts. In Escherichia coli , YidC plays a key role in the integration and assembly of many inner membrane proteins. Interestingly, YidC functions both in concert with the Sec‐translocon and as a separate insertase independent of the translocon. Mitochondria of higher eukaryotes contain two distant homologues of YidC: Oxa1 and Cox18/Oxa2. Oxa1 is required for the insertion of membrane proteins into the mitochondrial inner membrane. Cox18/Oxa2 plays a poorly defined role in the biogenesis of the cytochrome c oxidase complex. Employing a genetic complementation approach by expressing the conserved region of yeast Cox18 in E. coli , we show here that Cox18 is able to complement the essential Sec‐independent function of YidC. This identifies Cox18 as a bona fide member of the YidC/Oxa1/Alb3 family.