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YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase.
EMBO J 2000; 19(4):542-9EJ

Abstract

In Escherichia coli, both secretory and inner membrane proteins initially are targeted to the core SecYEG inner membrane translocase. Previous work has also identified the peripherally associated SecA protein as well as the SecD, SecF and YajC inner membrane proteins as components of the translocase. Here, we use a cross-linking approach to show that hydrophilic portions of a co-translationally targeted inner membrane protein (FtsQ) are close to SecA and SecY, suggesting that insertion takes place at the SecA/Y interface. The hydrophobic FtsQ signal anchor sequence contacts both lipids and a novel 60 kDa translocase-associated component that we identify as YidC. YidC is homologous to Saccharomyces cerevisiae Oxa1p, which has been shown to function in a novel export pathway at the mitochondrial inner membrane. We propose that YidC is involved in the insertion of hydrophobic sequences into the lipid bilayer after initial recognition by the SecAYEG translocase.

Authors+Show Affiliations

Department of Microbiology, Institute of Molecular Biological Sciences, Biocentrum Amsterdam, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10675323

Citation

Scotti, P A., et al. "YidC, the Escherichia Coli Homologue of Mitochondrial Oxa1p, Is a Component of the Sec Translocase." The EMBO Journal, vol. 19, no. 4, 2000, pp. 542-9.
Scotti PA, Urbanus ML, Brunner J, et al. YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 2000;19(4):542-9.
Scotti, P. A., Urbanus, M. L., Brunner, J., de Gier, J. W., von Heijne, G., van der Does, C., ... Luirink, J. (2000). YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. The EMBO Journal, 19(4), pp. 542-9.
Scotti PA, et al. YidC, the Escherichia Coli Homologue of Mitochondrial Oxa1p, Is a Component of the Sec Translocase. EMBO J. 2000 Feb 15;19(4):542-9. PubMed PMID: 10675323.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. AU - Scotti,P A, AU - Urbanus,M L, AU - Brunner,J, AU - de Gier,J W, AU - von Heijne,G, AU - van der Does,C, AU - Driessen,A J, AU - Oudega,B, AU - Luirink,J, PY - 2000/2/17/pubmed PY - 2000/3/25/medline PY - 2000/2/17/entrez SP - 542 EP - 9 JF - The EMBO journal JO - EMBO J. VL - 19 IS - 4 N2 - In Escherichia coli, both secretory and inner membrane proteins initially are targeted to the core SecYEG inner membrane translocase. Previous work has also identified the peripherally associated SecA protein as well as the SecD, SecF and YajC inner membrane proteins as components of the translocase. Here, we use a cross-linking approach to show that hydrophilic portions of a co-translationally targeted inner membrane protein (FtsQ) are close to SecA and SecY, suggesting that insertion takes place at the SecA/Y interface. The hydrophobic FtsQ signal anchor sequence contacts both lipids and a novel 60 kDa translocase-associated component that we identify as YidC. YidC is homologous to Saccharomyces cerevisiae Oxa1p, which has been shown to function in a novel export pathway at the mitochondrial inner membrane. We propose that YidC is involved in the insertion of hydrophobic sequences into the lipid bilayer after initial recognition by the SecAYEG translocase. SN - 0261-4189 UR - https://www.unboundmedicine.com/medline/citation/10675323/YidC_the_Escherichia_coli_homologue_of_mitochondrial_Oxa1p_is_a_component_of_the_Sec_translocase_ L2 - http://emboj.embopress.org/cgi/pmidlookup?view=long&pmid=10675323 DB - PRIME DP - Unbound Medicine ER -