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Targeting of proteins to the twin‐arginine translocation pathway

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. Th...

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Detalles Bibliográficos
Autores principales: Palmer, Tracy, Stansfeld, Phillip J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7317946/
https://www.ncbi.nlm.nih.gov/pubmed/31971282
http://dx.doi.org/10.1111/mmi.14461
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author Palmer, Tracy
Stansfeld, Phillip J.
author_facet Palmer, Tracy
Stansfeld, Phillip J.
author_sort Palmer, Tracy
collection PubMed
description 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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spelling pubmed-73179462020-06-29 Targeting of proteins to the twin‐arginine translocation pathway Palmer, Tracy Stansfeld, Phillip J. Mol Microbiol Microreviews 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. John Wiley and Sons Inc. 2020-02-20 2020-05 /pmc/articles/PMC7317946/ /pubmed/31971282 http://dx.doi.org/10.1111/mmi.14461 Text en © 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Microreviews
Palmer, Tracy
Stansfeld, Phillip J.
Targeting of proteins to the twin‐arginine translocation pathway
title Targeting of proteins to the twin‐arginine translocation pathway
title_full Targeting of proteins to the twin‐arginine translocation pathway
title_fullStr Targeting of proteins to the twin‐arginine translocation pathway
title_full_unstemmed Targeting of proteins to the twin‐arginine translocation pathway
title_short Targeting of proteins to the twin‐arginine translocation pathway
title_sort targeting of proteins to the twin‐arginine translocation pathway
topic Microreviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7317946/
https://www.ncbi.nlm.nih.gov/pubmed/31971282
http://dx.doi.org/10.1111/mmi.14461
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