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Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.
Proc Natl Acad Sci U S A 2014; 111(13):4844-9PN

Abstract

The SecY/61 complex forms the protein-channel component of the ubiquitous protein secretion and membrane protein insertion apparatus. The bacterial version SecYEG interacts with the highly conserved YidC and SecDF-YajC subcomplex, which facilitates translocation into and across the membrane. Together, they form the holo-translocon (HTL), which we have successfully overexpressed and purified. In contrast to the homo-dimeric SecYEG, the HTL is a hetero-dimer composed of single copies of SecYEG and SecDF-YajC-YidC. The activities of the HTL differ from the archetypal SecYEG complex. It is more effective in cotranslational insertion of membrane proteins and the posttranslational secretion of a β-barreled outer-membrane protein driven by SecA and ATP becomes much more dependent on the proton-motive force. The activity of the translocating copy of SecYEG may therefore be modulated by association with different accessory subcomplexes: SecYEG (forming SecYEG dimers) or SecDF-YajC-YidC (forming the HTL). This versatility may provide a means to refine the secretion and insertion capabilities according to the substrate. A similar modularity may also be exploited for the translocation or insertion of a wide range of substrates across and into the endoplasmic reticular and mitochondrial membranes of eukaryotes.

Authors+Show Affiliations

School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.No affiliation info availableNo affiliation info availableNo 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)

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

Language

eng

PubMed ID

24550475

Citation

Schulze, Ryan J., et al. "Membrane Protein Insertion and Proton-motive-force-dependent Secretion Through the Bacterial Holo-translocon SecYEG-SecDF-YajC-YidC." Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 13, 2014, pp. 4844-9.
Schulze RJ, Komar J, Botte M, et al. Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. Proc Natl Acad Sci USA. 2014;111(13):4844-9.
Schulze, R. J., Komar, J., Botte, M., Allen, W. J., Whitehouse, S., Gold, V. A., ... Collinson, I. (2014). Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. Proceedings of the National Academy of Sciences of the United States of America, 111(13), pp. 4844-9. doi:10.1073/pnas.1315901111.
Schulze RJ, et al. Membrane Protein Insertion and Proton-motive-force-dependent Secretion Through the Bacterial Holo-translocon SecYEG-SecDF-YajC-YidC. Proc Natl Acad Sci USA. 2014 Apr 1;111(13):4844-9. PubMed PMID: 24550475.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. AU - Schulze,Ryan J, AU - Komar,Joanna, AU - Botte,Mathieu, AU - Allen,William J, AU - Whitehouse,Sarah, AU - Gold,Vicki A M, AU - Lycklama A Nijeholt,Jelger A, AU - Huard,Karine, AU - Berger,Imre, AU - Schaffitzel,Christiane, AU - Collinson,Ian, Y1 - 2014/02/18/ PY - 2014/2/20/entrez PY - 2014/2/20/pubmed PY - 2014/6/3/medline SP - 4844 EP - 9 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc. Natl. Acad. Sci. U.S.A. VL - 111 IS - 13 N2 - The SecY/61 complex forms the protein-channel component of the ubiquitous protein secretion and membrane protein insertion apparatus. The bacterial version SecYEG interacts with the highly conserved YidC and SecDF-YajC subcomplex, which facilitates translocation into and across the membrane. Together, they form the holo-translocon (HTL), which we have successfully overexpressed and purified. In contrast to the homo-dimeric SecYEG, the HTL is a hetero-dimer composed of single copies of SecYEG and SecDF-YajC-YidC. The activities of the HTL differ from the archetypal SecYEG complex. It is more effective in cotranslational insertion of membrane proteins and the posttranslational secretion of a β-barreled outer-membrane protein driven by SecA and ATP becomes much more dependent on the proton-motive force. The activity of the translocating copy of SecYEG may therefore be modulated by association with different accessory subcomplexes: SecYEG (forming SecYEG dimers) or SecDF-YajC-YidC (forming the HTL). This versatility may provide a means to refine the secretion and insertion capabilities according to the substrate. A similar modularity may also be exploited for the translocation or insertion of a wide range of substrates across and into the endoplasmic reticular and mitochondrial membranes of eukaryotes. SN - 1091-6490 UR - https://www.unboundmedicine.com/medline/citation/24550475/Membrane_protein_insertion_and_proton_motive_force_dependent_secretion_through_the_bacterial_holo_translocon_SecYEG_SecDF_YajC_YidC_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=24550475 DB - PRIME DP - Unbound Medicine ER -