Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.

The twin-arginine translocation (Tat) pathway transports folded proteins across energetic membranes. Numerous Tat substrates contain co-factors that are inserted before transport with the assistance of redox enzyme maturation proteins (REMPs), which bind to the signal peptide of precursor proteins....

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Autores principales:	Umesh K Bageshwar, Antara DattaGupta, Siegfried M Musser
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/855777d3fd5742e18146a187370c6a7e
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spelling	oai:doaj.org-article:855777d3fd5742e18146a187370c6a7e2021-12-02T20:08:23ZInfluence of the TorD signal peptide chaperone on Tat-dependent protein translocation.1932-620310.1371/journal.pone.0256715https://doaj.org/article/855777d3fd5742e18146a187370c6a7e2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0256715https://doaj.org/toc/1932-6203The twin-arginine translocation (Tat) pathway transports folded proteins across energetic membranes. Numerous Tat substrates contain co-factors that are inserted before transport with the assistance of redox enzyme maturation proteins (REMPs), which bind to the signal peptide of precursor proteins. How signal peptides are transferred from a REMP to a binding site on the Tat receptor complex remains unknown. Since the signal peptide mediates both interactions, possibilities include: i) a coordinated hand-off mechanism; or ii) a diffusional search after REMP dissociation. We investigated the binding interaction between substrates containing the TorA signal peptide (spTorA) and its cognate REMP, TorD, and the effect of TorD on the in vitro transport of such substrates. We found that Escherichia coli TorD is predominantly a monomer at low micromolar concentrations (dimerization KD > 50 μM), and this monomer binds reversibly to spTorA (KD ≈ 1 μM). While TorD binds to membranes (KD ≈ 100 nM), it has no apparent affinity for Tat translocons and it inhibits binding of a precursor substrate to the membrane. TorD has a minimal effect on substrate transport by the Tat system, being mildly inhibitory at high concentrations. These data are consistent with a model in which the REMP-bound signal peptide is shielded from recognition by the Tat translocon, and spontaneous dissociation of the REMP allows the substrate to engage the Tat machinery. Thus, the REMP does not assist with targeting to the Tat translocon, but rather temporarily shields the signal peptide.Umesh K BageshwarAntara DattaGuptaSiegfried M MusserPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 9, p e0256715 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Umesh K Bageshwar Antara DattaGupta Siegfried M Musser Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
description	The twin-arginine translocation (Tat) pathway transports folded proteins across energetic membranes. Numerous Tat substrates contain co-factors that are inserted before transport with the assistance of redox enzyme maturation proteins (REMPs), which bind to the signal peptide of precursor proteins. How signal peptides are transferred from a REMP to a binding site on the Tat receptor complex remains unknown. Since the signal peptide mediates both interactions, possibilities include: i) a coordinated hand-off mechanism; or ii) a diffusional search after REMP dissociation. We investigated the binding interaction between substrates containing the TorA signal peptide (spTorA) and its cognate REMP, TorD, and the effect of TorD on the in vitro transport of such substrates. We found that Escherichia coli TorD is predominantly a monomer at low micromolar concentrations (dimerization KD > 50 μM), and this monomer binds reversibly to spTorA (KD ≈ 1 μM). While TorD binds to membranes (KD ≈ 100 nM), it has no apparent affinity for Tat translocons and it inhibits binding of a precursor substrate to the membrane. TorD has a minimal effect on substrate transport by the Tat system, being mildly inhibitory at high concentrations. These data are consistent with a model in which the REMP-bound signal peptide is shielded from recognition by the Tat translocon, and spontaneous dissociation of the REMP allows the substrate to engage the Tat machinery. Thus, the REMP does not assist with targeting to the Tat translocon, but rather temporarily shields the signal peptide.
format	article
author	Umesh K Bageshwar Antara DattaGupta Siegfried M Musser
author_facet	Umesh K Bageshwar Antara DattaGupta Siegfried M Musser
author_sort	Umesh K Bageshwar
title	Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
title_short	Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
title_full	Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
title_fullStr	Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
title_full_unstemmed	Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
title_sort	influence of the tord signal peptide chaperone on tat-dependent protein translocation.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/855777d3fd5742e18146a187370c6a7e
work_keys_str_mv	AT umeshkbageshwar influenceofthetordsignalpeptidechaperoneontatdependentproteintranslocation AT antaradattagupta influenceofthetordsignalpeptidechaperoneontatdependentproteintranslocation AT siegfriedmmusser influenceofthetordsignalpeptidechaperoneontatdependentproteintranslocation
_version_	1718375193324290048

Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.

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