Unanticipated functional diversity among the TatA-type components of the Tat protein translocase

Abstract Twin-arginine translocation (Tat) systems transport folded proteins that harbor a conserved arginine pair in their signal peptides. They assemble from hexahelical TatC-type and single-spanning TatA-type proteins. Many Tat systems comprise two functionally diverse, TatA-type proteins, denomi...

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Autores principales:	Ekaterina Eimer, Wei-Chun Kao, Julia Fröbel, Anne-Sophie Blümmel, Carola Hunte, Matthias Müller
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/70cbc1deb7b64855b146cb9bf3d148ff
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spelling	oai:doaj.org-article:70cbc1deb7b64855b146cb9bf3d148ff2021-12-02T15:08:25ZUnanticipated functional diversity among the TatA-type components of the Tat protein translocase10.1038/s41598-018-19640-32045-2322https://doaj.org/article/70cbc1deb7b64855b146cb9bf3d148ff2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-19640-3https://doaj.org/toc/2045-2322Abstract Twin-arginine translocation (Tat) systems transport folded proteins that harbor a conserved arginine pair in their signal peptides. They assemble from hexahelical TatC-type and single-spanning TatA-type proteins. Many Tat systems comprise two functionally diverse, TatA-type proteins, denominated TatA and TatB. Some bacteria in addition express TatE, which thus far has been characterized as a functional surrogate of TatA. For the Tat system of Escherichia coli we demonstrate here that different from TatA but rather like TatB, TatE contacts a Tat signal peptide independently of the proton-motive force and restricts the premature processing of a Tat signal peptide. Furthermore, TatE embarks at the transmembrane helix five of TatC where it becomes so closely spaced to TatB that both proteins can be covalently linked by a zero-space cross-linker. Our results suggest that in addition to TatB and TatC, TatE is a further component of the Tat substrate receptor complex. Consistent with TatE being an autonomous TatAB-type protein, a bioinformatics analysis revealed a relatively broad distribution of the tatE gene in bacterial phyla and highlighted unique protein sequence features of TatE orthologs.Ekaterina EimerWei-Chun KaoJulia FröbelAnne-Sophie BlümmelCarola HunteMatthias MüllerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ekaterina Eimer Wei-Chun Kao Julia Fröbel Anne-Sophie Blümmel Carola Hunte Matthias Müller Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
description	Abstract Twin-arginine translocation (Tat) systems transport folded proteins that harbor a conserved arginine pair in their signal peptides. They assemble from hexahelical TatC-type and single-spanning TatA-type proteins. Many Tat systems comprise two functionally diverse, TatA-type proteins, denominated TatA and TatB. Some bacteria in addition express TatE, which thus far has been characterized as a functional surrogate of TatA. For the Tat system of Escherichia coli we demonstrate here that different from TatA but rather like TatB, TatE contacts a Tat signal peptide independently of the proton-motive force and restricts the premature processing of a Tat signal peptide. Furthermore, TatE embarks at the transmembrane helix five of TatC where it becomes so closely spaced to TatB that both proteins can be covalently linked by a zero-space cross-linker. Our results suggest that in addition to TatB and TatC, TatE is a further component of the Tat substrate receptor complex. Consistent with TatE being an autonomous TatAB-type protein, a bioinformatics analysis revealed a relatively broad distribution of the tatE gene in bacterial phyla and highlighted unique protein sequence features of TatE orthologs.
format	article
author	Ekaterina Eimer Wei-Chun Kao Julia Fröbel Anne-Sophie Blümmel Carola Hunte Matthias Müller
author_facet	Ekaterina Eimer Wei-Chun Kao Julia Fröbel Anne-Sophie Blümmel Carola Hunte Matthias Müller
author_sort	Ekaterina Eimer
title	Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
title_short	Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
title_full	Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
title_fullStr	Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
title_full_unstemmed	Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
title_sort	unanticipated functional diversity among the tata-type components of the tat protein translocase
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/70cbc1deb7b64855b146cb9bf3d148ff
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Unanticipated functional diversity among the TatA-type components of the Tat protein translocase

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