The protease GtgE from Salmonella exclusively targets inactive Rab GTPases

The bacterial protease GtgE is involved in the establishment of Salmonellosis. Here the authors provide a structural and biochemical analysis of GtgE that sheds light on the molecular mechanisms of reprogramming infected host cells via site-specific proteolytic cleavage of the vesicular trafficking...

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Main Authors:	Rudolf Wachtel, Bastian Bräuning, Sophie L. Mader, Felix Ecker, Ville R. I. Kaila, Michael Groll, Aymelt Itzen
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-01-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-02110-1

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spelling	doaj-b1737a5a57314d0189c7e7ac298e88462021-05-11T09:23:04ZengNature Publishing GroupNature Communications2041-17232018-01-019111310.1038/s41467-017-02110-1The protease GtgE from Salmonella exclusively targets inactive Rab GTPasesRudolf Wachtel0Bastian Bräuning1Sophie L. Mader2Felix Ecker3Ville R. I. Kaila4Michael Groll5Aymelt Itzen6Center for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichCenter for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of MunichThe bacterial protease GtgE is involved in the establishment of Salmonellosis. Here the authors provide a structural and biochemical analysis of GtgE that sheds light on the molecular mechanisms of reprogramming infected host cells via site-specific proteolytic cleavage of the vesicular trafficking regulator Rab32.https://doi.org/10.1038/s41467-017-02110-1
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Rudolf Wachtel Bastian Bräuning Sophie L. Mader Felix Ecker Ville R. I. Kaila Michael Groll Aymelt Itzen
spellingShingle	Rudolf Wachtel Bastian Bräuning Sophie L. Mader Felix Ecker Ville R. I. Kaila Michael Groll Aymelt Itzen The protease GtgE from Salmonella exclusively targets inactive Rab GTPases Nature Communications
author_facet	Rudolf Wachtel Bastian Bräuning Sophie L. Mader Felix Ecker Ville R. I. Kaila Michael Groll Aymelt Itzen
author_sort	Rudolf Wachtel
title	The protease GtgE from Salmonella exclusively targets inactive Rab GTPases
title_short	The protease GtgE from Salmonella exclusively targets inactive Rab GTPases
title_full	The protease GtgE from Salmonella exclusively targets inactive Rab GTPases
title_fullStr	The protease GtgE from Salmonella exclusively targets inactive Rab GTPases
title_full_unstemmed	The protease GtgE from Salmonella exclusively targets inactive Rab GTPases
title_sort	protease gtge from salmonella exclusively targets inactive rab gtpases
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-01-01
description	The bacterial protease GtgE is involved in the establishment of Salmonellosis. Here the authors provide a structural and biochemical analysis of GtgE that sheds light on the molecular mechanisms of reprogramming infected host cells via site-specific proteolytic cleavage of the vesicular trafficking regulator Rab32.
url	https://doi.org/10.1038/s41467-017-02110-1
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The protease GtgE from Salmonella exclusively targets inactive Rab GTPases

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