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Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA.
J Biol Chem 2006; 281(15):10002-9JB

Abstract

Inner membrane proteins (IMPs) of Escherichia coli use different pathways for membrane targeting and integration. YidC plays an essential but poorly defined role in the integration and folding of IMPs both in conjunction with the Sec translocon and as a Sec-independent insertase. Depletion of YidC only marginally affects the insertion of Sec-dependent IMPs, whereas it blocks the insertion of a subset of Sec-independent IMPs. Substrates of this latter "YidC-only" pathway include the relatively small IMPs M13 procoat, Pf3 coat protein, and subunit c of the F(1)F(0) ATPase. Recently, it has been shown that the steady state level of the larger and more complex CyoA subunit of the cytochrome o oxidase is also severely affected upon depletion of YidC. In the present study we have analyzed the biogenesis of the integral lipoprotein CyoA. Collectively, our data suggest that the first transmembrane segment of CyoA rather than the signal sequence recruits the signal recognition particle for membrane targeting. Membrane integration and assembly appear to occur in two distinct sequential steps. YidC is sufficient to catalyze insertion of the N-terminal domain consisting of the signal sequence, transmembrane segment 1, and the small periplasmic domain in between. Translocation of the large C-terminal periplasmic domain requires the Sec translocon and SecA, suggesting that for this particular IMP the Sec translocon might operate downstream of YidC.

Authors+Show Affiliations

Department of Molecular Microbiology, Institute of Molecular Cell Biology, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16481320

Citation

van Bloois, Edwin, et al. "Distinct Requirements for Translocation of the N-tail and C-tail of the Escherichia Coli Inner Membrane Protein CyoA." The Journal of Biological Chemistry, vol. 281, no. 15, 2006, pp. 10002-9.
van Bloois E, Haan GJ, de Gier JW, et al. Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. J Biol Chem. 2006;281(15):10002-9.
van Bloois, E., Haan, G. J., de Gier, J. W., Oudega, B., & Luirink, J. (2006). Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. The Journal of Biological Chemistry, 281(15), pp. 10002-9.
van Bloois E, et al. Distinct Requirements for Translocation of the N-tail and C-tail of the Escherichia Coli Inner Membrane Protein CyoA. J Biol Chem. 2006 Apr 14;281(15):10002-9. PubMed PMID: 16481320.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. AU - van Bloois,Edwin, AU - Haan,Gert-Jan, AU - de Gier,Jan-Willem, AU - Oudega,Bauke, AU - Luirink,Joen, Y1 - 2006/02/15/ PY - 2006/2/17/pubmed PY - 2006/6/6/medline PY - 2006/2/17/entrez SP - 10002 EP - 9 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 281 IS - 15 N2 - Inner membrane proteins (IMPs) of Escherichia coli use different pathways for membrane targeting and integration. YidC plays an essential but poorly defined role in the integration and folding of IMPs both in conjunction with the Sec translocon and as a Sec-independent insertase. Depletion of YidC only marginally affects the insertion of Sec-dependent IMPs, whereas it blocks the insertion of a subset of Sec-independent IMPs. Substrates of this latter "YidC-only" pathway include the relatively small IMPs M13 procoat, Pf3 coat protein, and subunit c of the F(1)F(0) ATPase. Recently, it has been shown that the steady state level of the larger and more complex CyoA subunit of the cytochrome o oxidase is also severely affected upon depletion of YidC. In the present study we have analyzed the biogenesis of the integral lipoprotein CyoA. Collectively, our data suggest that the first transmembrane segment of CyoA rather than the signal sequence recruits the signal recognition particle for membrane targeting. Membrane integration and assembly appear to occur in two distinct sequential steps. YidC is sufficient to catalyze insertion of the N-terminal domain consisting of the signal sequence, transmembrane segment 1, and the small periplasmic domain in between. Translocation of the large C-terminal periplasmic domain requires the Sec translocon and SecA, suggesting that for this particular IMP the Sec translocon might operate downstream of YidC. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/16481320/Distinct_requirements_for_translocation_of_the_N_tail_and_C_tail_of_the_Escherichia_coli_inner_membrane_protein_CyoA_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=16481320 DB - PRIME DP - Unbound Medicine ER -