Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems

Many bacteria export effector proteins even when two incompatible signal sequences are present, one which would lead to export and the other to inner membrane targeting. Here the authors show that such proteins feature decreased hydrophobicity or cognate chaperone binding to prevent erroneous target...

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Autores principales:	Lea Krampen, Silke Malmsheimer, Iwan Grin, Thomas Trunk, Anja Lührmann, Jan-Willem de Gier, Samuel Wagner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/864e25c152e74479baf43777512bbf77
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spelling	oai:doaj.org-article:864e25c152e74479baf43777512bbf772021-12-02T17:31:57ZRevealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems10.1038/s41467-018-05969-w2041-1723https://doaj.org/article/864e25c152e74479baf43777512bbf772018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05969-whttps://doaj.org/toc/2041-1723Many bacteria export effector proteins even when two incompatible signal sequences are present, one which would lead to export and the other to inner membrane targeting. Here the authors show that such proteins feature decreased hydrophobicity or cognate chaperone binding to prevent erroneous targeting.Lea KrampenSilke MalmsheimerIwan GrinThomas TrunkAnja LührmannJan-Willem de GierSamuel WagnerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lea Krampen Silke Malmsheimer Iwan Grin Thomas Trunk Anja Lührmann Jan-Willem de Gier Samuel Wagner Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
description	Many bacteria export effector proteins even when two incompatible signal sequences are present, one which would lead to export and the other to inner membrane targeting. Here the authors show that such proteins feature decreased hydrophobicity or cognate chaperone binding to prevent erroneous targeting.
format	article
author	Lea Krampen Silke Malmsheimer Iwan Grin Thomas Trunk Anja Lührmann Jan-Willem de Gier Samuel Wagner
author_facet	Lea Krampen Silke Malmsheimer Iwan Grin Thomas Trunk Anja Lührmann Jan-Willem de Gier Samuel Wagner
author_sort	Lea Krampen
title	Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
title_short	Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
title_full	Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
title_fullStr	Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
title_full_unstemmed	Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
title_sort	revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/864e25c152e74479baf43777512bbf77
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Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems

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