Targeting of proteins to the twin-arginine translocation pathway

Tracy Palmer; Phillip J. Stansfeld

doi:10.1111/mmi.14461

Targeting of proteins to the twin-arginine translocation pathway

Tracy Palmer (Lead / Corresponding author), Phillip J. Stansfeld

DArcy Thompson Unit

Research output: Contribution to journal › Review article › peer-review

46 Citations (Scopus)

70 Downloads (Pure)

Abstract

The twin-arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N-terminal signal sequence containing a highly conserved twin-arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.

Original language	English
Pages (from-to)	861-871
Number of pages	11
Journal	Molecular Microbiology
Volume	113
Issue number	5
Early online date	23 Jan 2020
DOIs	https://doi.org/10.1111/mmi.14461
Publication status	Published - May 2020

Keywords

folded protein
mechanism
protein transport
Tat pathway
twin-arginine signal peptide

ASJC Scopus subject areas

Microbiology
Molecular Biology

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10.1111/mmi.14461

Final Published VersionFinal published version, 1.35 MBLicence: CC BY

Cite this

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title = "Targeting of proteins to the twin-arginine translocation pathway",

abstract = "The twin-arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N-terminal signal sequence containing a highly conserved twin-arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.",

keywords = "folded protein, mechanism, protein transport, Tat pathway, twin-arginine signal peptide",

author = "Tracy Palmer and Stansfeld, {Phillip J.}",

note = "Funding Information: We thank Professor Ben Berks (University of Oxford) for critical comments on the manuscript. Work in the authors' laboratories is supported by the UK Research and Innovation Medical Research Council through grant MR/S009213/1 and the the Biotechnology and Biological Sciences Research council [grants BB/S005307/1, BB/N014545/1 BB/P01948X/1, BB/R002517/1 and BB/S003339/1] and by Wellcome [110183/A/15/Z and 208361/Z/17/Z]. We would also like to thank the UK High-End Computing Consortium for Biomolecular Simulation, HECBioSim, for providing time on ARCHER (http://hecbiosim.ac.uk), supported by EPSRC (grant no. EP/R029407/1). Publisher Copyright: {\textcopyright} 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "2020",

month = may,

doi = "10.1111/mmi.14461",

language = "English",

volume = "113",

pages = "861--871",

journal = "Molecular Microbiology",

issn = "0950-382X",

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AU - Palmer, Tracy

AU - Stansfeld, Phillip J.

N1 - Funding Information: We thank Professor Ben Berks (University of Oxford) for critical comments on the manuscript. Work in the authors' laboratories is supported by the UK Research and Innovation Medical Research Council through grant MR/S009213/1 and the the Biotechnology and Biological Sciences Research council [grants BB/S005307/1, BB/N014545/1 BB/P01948X/1, BB/R002517/1 and BB/S003339/1] and by Wellcome [110183/A/15/Z and 208361/Z/17/Z]. We would also like to thank the UK High-End Computing Consortium for Biomolecular Simulation, HECBioSim, for providing time on ARCHER (http://hecbiosim.ac.uk), supported by EPSRC (grant no. EP/R029407/1). Publisher Copyright: © 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 2020/5

Y1 - 2020/5

N2 - The twin-arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N-terminal signal sequence containing a highly conserved twin-arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.

AB - The twin-arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N-terminal signal sequence containing a highly conserved twin-arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.

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KW - twin-arginine signal peptide

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JF - Molecular Microbiology

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Targeting of proteins to the twin-arginine translocation pathway

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Identification of Substrates and Roles in Virulence of the Staphylococcus Aureus Ess Protein Secretion System (Investigator Award)

Characterisation of the Assembled State of the Tat Protein Transport System

Co-Ordinating Different Protein Translocation Machineries During Assembly of a Membrane Protein

Cite this

Targeting of proteins to the twin-arginine translocation pathway

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Projects

Identification of Substrates and Roles in Virulence of the Staphylococcus Aureus Ess Protein Secretion System (Investigator Award)

Characterisation of the Assembled State of the Tat Protein Transport System

Co-Ordinating Different Protein Translocation Machineries During Assembly of a Membrane Protein

Cite this