How to achieve Tat transport with alien TatA

Abstract TatA is an essential and structurally conserved component of all known Twin-arginine transport (Tat) machineries which are able to catalyse membrane transport of fully folded proteins. Here we have investigated if bacterial TatA, or chimeric pea/E. coli TatA derivatives, are capable of repl...

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Autores principales:	René Steffen Hauer, Roland Freudl, Julia Dittmar, Mario Jakob, Ralf Bernd Klösgen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c80b94c7c1954b129841cd8a44c5f7e8
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id	oai:doaj.org-article:c80b94c7c1954b129841cd8a44c5f7e8
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spelling	oai:doaj.org-article:c80b94c7c1954b129841cd8a44c5f7e82021-12-02T15:06:09ZHow to achieve Tat transport with alien TatA10.1038/s41598-017-08818-w2045-2322https://doaj.org/article/c80b94c7c1954b129841cd8a44c5f7e82017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08818-whttps://doaj.org/toc/2045-2322Abstract TatA is an essential and structurally conserved component of all known Twin-arginine transport (Tat) machineries which are able to catalyse membrane transport of fully folded proteins. Here we have investigated if bacterial TatA, or chimeric pea/E. coli TatA derivatives, are capable of replacing thylakoidal TatA in function. While authentic E. coli TatA does not show any transport activity in thylakoid transport experiments, TatA chimeras comprising the transmembrane helix (TMH) of pea TatA are fully active. For minimal catalytic activity it is even sufficient to replace three residues within TMH of E. coli TatA by the corresponding pea residues. Almost any further substitution within TMH gradually raises transport activity in the thylakoid system, while functional characterization of the same set of TatA derivatives in E. coli yields essentially inverse catalytic activities. Closer inspection of the substituted residues suggests that the two transport systems have deviating demands with regard to the hydrophobicity of the transmembrane helix.René Steffen HauerRoland FreudlJulia DittmarMario JakobRalf Bernd KlösgenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q René Steffen Hauer Roland Freudl Julia Dittmar Mario Jakob Ralf Bernd Klösgen How to achieve Tat transport with alien TatA
description	Abstract TatA is an essential and structurally conserved component of all known Twin-arginine transport (Tat) machineries which are able to catalyse membrane transport of fully folded proteins. Here we have investigated if bacterial TatA, or chimeric pea/E. coli TatA derivatives, are capable of replacing thylakoidal TatA in function. While authentic E. coli TatA does not show any transport activity in thylakoid transport experiments, TatA chimeras comprising the transmembrane helix (TMH) of pea TatA are fully active. For minimal catalytic activity it is even sufficient to replace three residues within TMH of E. coli TatA by the corresponding pea residues. Almost any further substitution within TMH gradually raises transport activity in the thylakoid system, while functional characterization of the same set of TatA derivatives in E. coli yields essentially inverse catalytic activities. Closer inspection of the substituted residues suggests that the two transport systems have deviating demands with regard to the hydrophobicity of the transmembrane helix.
format	article
author	René Steffen Hauer Roland Freudl Julia Dittmar Mario Jakob Ralf Bernd Klösgen
author_facet	René Steffen Hauer Roland Freudl Julia Dittmar Mario Jakob Ralf Bernd Klösgen
author_sort	René Steffen Hauer
title	How to achieve Tat transport with alien TatA
title_short	How to achieve Tat transport with alien TatA
title_full	How to achieve Tat transport with alien TatA
title_fullStr	How to achieve Tat transport with alien TatA
title_full_unstemmed	How to achieve Tat transport with alien TatA
title_sort	how to achieve tat transport with alien tata
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/c80b94c7c1954b129841cd8a44c5f7e8
work_keys_str_mv	AT renesteffenhauer howtoachievetattransportwithalientata AT rolandfreudl howtoachievetattransportwithalientata AT juliadittmar howtoachievetattransportwithalientata AT mariojakob howtoachievetattransportwithalientata AT ralfberndklosgen howtoachievetattransportwithalientata
_version_	1718388609798635520

How to achieve Tat transport with alien TatA

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