Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC

Joanna Komar; Sara Alvira-de-Celis; Ryan Schulze; Remy Martin; Jelger A. Lycklama A. Nijeholtb; S Lee; Timothy Dafforn; Gabriele Deckers-Hebestreit; Imre Berger; Christiane Schaffitzel; Ian Collinson

doi:10.1042/BCJ20160545

Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC

Joanna Komar, Sara Alvira-de-Celis, Ryan Schulze, Remy Martin, Jelger A. Lycklama A. Nijeholtb, S Lee, Timothy Dafforn, Gabriele Deckers-Hebestreit, Imre Berger, Christiane Schaffitzel, Ian Collinson

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Abstract

Protein secretion and membrane insertion occurs through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea) / Sec61 (eukaryotes) translocon. A common mechanism then guides nascent trans-membrane helices (TMHs) through the Sec complex, mediated by associated membrane insertion factors. In bacteria, the membrane protein 'insertase' YidC ushers TMHs through a lateral gate of SecY to the bilayer. YidC is also thought to incorporate proteins into the membrane independently of SecYEG. Here, we show the bacterial holo-translocon (HTL) - a super-complex of SecYEG-SecDF-YajC-YidC - is a bona fide resident of the E. coli inner membrane. Moreover, when compared to SecYEG and YidC alone, the HTL is more effective at the insertion and assembly of a wide range of membrane protein substrates, including those hitherto thought to require only YidC.

Original language	English
Pages (from-to)	3341-3354
Number of pages	14
Journal	Biochemical Journal
Volume	473
Early online date	27 Sept 2016
DOIs	https://doi.org/10.1042/BCJ20160545
Publication status	Published - Oct 2016

Research Groups and Themes

Bristol BioDesign Institute
BrisSynBio

Keywords

synthetic biology

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10.1042/BCJ20160545

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This is the final published version of the article (version of record). It first appeared online via Portland Press at http://www.biochemj.org/content/473/19/3341. Please refer to any applicable terms of use of the publisher.
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This is the final published version of the article (version of record). It first appeared online via Portland Press at http://www.biochemj.org/content/473/19/3341. Please refer to any applicable terms of use of the publisher.
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Understanding the Mechanism of Membrane Protein Insertion
Collinson, I. R. (Principal Investigator)
1/10/14 → 28/02/18
Project: Research
ANALYSIS OF THE INTERACTION BETWEEN THE SECY PROTEIN TRANSLOCATION COMPLEX AND IT'S SUBSTRATE SIGNAL SEQUENCE (HULL CO-APPLICANT)
Collinson, I. R. (Principal Investigator)
1/12/07 → 1/12/11
Project: Research

Professor Ian R Collinson
- Ian.Collinsonbristol.acuk
- School of Biochemistry - Professor of Biochemistry
Person: Academic

Cite this

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title = "Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC",

abstract = "Protein secretion and membrane insertion occurs through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea) / Sec61 (eukaryotes) translocon. A common mechanism then guides nascent trans-membrane helices (TMHs) through the Sec complex, mediated by associated membrane insertion factors. In bacteria, the membrane protein 'insertase' YidC ushers TMHs through a lateral gate of SecY to the bilayer. YidC is also thought to incorporate proteins into the membrane independently of SecYEG. Here, we show the bacterial holo-translocon (HTL) - a super-complex of SecYEG-SecDF-YajC-YidC - is a bona fide resident of the E. coli inner membrane. Moreover, when compared to SecYEG and YidC alone, the HTL is more effective at the insertion and assembly of a wide range of membrane protein substrates, including those hitherto thought to require only YidC.",

keywords = "synthetic biology",

author = "Joanna Komar and Sara Alvira-de-Celis and Ryan Schulze and Remy Martin and Nijeholtb, {Jelger A. Lycklama A.} and S Lee and Timothy Dafforn and Gabriele Deckers-Hebestreit and Imre Berger and Christiane Schaffitzel and Ian Collinson",

year = "2016",

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doi = "10.1042/BCJ20160545",

language = "English",

volume = "473",

pages = "3341--3354",

journal = "Biochemical Journal",

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AU - Komar, Joanna

AU - Alvira-de-Celis, Sara

AU - Schulze, Ryan

AU - Martin, Remy

AU - Nijeholtb, Jelger A. Lycklama A.

AU - Lee, S

AU - Dafforn, Timothy

AU - Deckers-Hebestreit, Gabriele

AU - Berger, Imre

AU - Schaffitzel, Christiane

AU - Collinson, Ian

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N2 - Protein secretion and membrane insertion occurs through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea) / Sec61 (eukaryotes) translocon. A common mechanism then guides nascent trans-membrane helices (TMHs) through the Sec complex, mediated by associated membrane insertion factors. In bacteria, the membrane protein 'insertase' YidC ushers TMHs through a lateral gate of SecY to the bilayer. YidC is also thought to incorporate proteins into the membrane independently of SecYEG. Here, we show the bacterial holo-translocon (HTL) - a super-complex of SecYEG-SecDF-YajC-YidC - is a bona fide resident of the E. coli inner membrane. Moreover, when compared to SecYEG and YidC alone, the HTL is more effective at the insertion and assembly of a wide range of membrane protein substrates, including those hitherto thought to require only YidC.

AB - Protein secretion and membrane insertion occurs through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea) / Sec61 (eukaryotes) translocon. A common mechanism then guides nascent trans-membrane helices (TMHs) through the Sec complex, mediated by associated membrane insertion factors. In bacteria, the membrane protein 'insertase' YidC ushers TMHs through a lateral gate of SecY to the bilayer. YidC is also thought to incorporate proteins into the membrane independently of SecYEG. Here, we show the bacterial holo-translocon (HTL) - a super-complex of SecYEG-SecDF-YajC-YidC - is a bona fide resident of the E. coli inner membrane. Moreover, when compared to SecYEG and YidC alone, the HTL is more effective at the insertion and assembly of a wide range of membrane protein substrates, including those hitherto thought to require only YidC.

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DO - 10.1042/BCJ20160545

M3 - Article (Academic Journal)

C2 - 27435098

SN - 0264-6021

VL - 473

SP - 3341

EP - 3354

JO - Biochemical Journal

JF - Biochemical Journal

ER -

Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC

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Understanding the Mechanism of Membrane Protein Insertion

ANALYSIS OF THE INTERACTION BETWEEN THE SECY PROTEIN TRANSLOCATION COMPLEX AND IT'S SUBSTRATE SIGNAL SEQUENCE (HULL CO-APPLICANT)

Profiles

Professor Ian R Collinson

Cite this