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YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly
Author(s) -
Luirink Joen,
Samuelsson Tore,
de Gier Jan-Willem
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02616-3
Subject(s) - translocon , inner membrane , twin arginine translocation pathway , membrane protein , microbiology and biotechnology , translocase of the inner membrane , endoplasmic reticulum , biology , thylakoid , protein targeting , membrane transport protein , integral membrane protein , chloroplast , mitochondrial membrane transport protein , intermembrane space , membrane , mitochondrion , biochemistry , bacterial outer membrane , escherichia coli , gene
This review focuses on a novel, evolutionarily conserved mediator of membrane protein assembly in bacteria, mitochondria and chloroplasts. This factor is designated YidC in Escherichia coli , and is localized in the inner membrane. YidC is homologous to Oxa1p in the mitochondrial inner membrane and Alb3 in the chloroplast thylakoid membrane, but does not seem to have a homologue in the endoplasmic reticulum membrane. It has been suggested that YidC operates both as a separate unit and in connection with the SecYEG‐translocon depending on the substrate membrane protein that is integrated into the membrane. Mitochondria do not possess a SecYEG‐like complex and Oxa1p is thought to form, or to contribute to the formation of, a novel translocon in the mitochondrial inner membrane. Alb3 in the chloroplast thylakoid membrane is, just like YidC and Oxa1p, involved in membrane protein assembly, but only few details are known.