Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin

Rearrangement hot spots (Rhs) proteins are bacterial polymorphic toxin systems. Here, the authors show that Rhs1 forms a complex with the Type VI secretion system (T6SS) spike protein VgrG and the EagR chaperone. They also present the cryo-EM structure of the Rhs1-EagR complex and propose a model fo...

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Autores principales: Dukas Jurėnas, Leonardo Talachia Rosa, Martial Rey, Julia Chamot-Rooke, Rémi Fronzes, Eric Cascales
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/3207bbe65e894dab9e6e7124d3c24849
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spelling oai:doaj.org-article:3207bbe65e894dab9e6e7124d3c248492021-12-05T12:21:59ZMounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin10.1038/s41467-021-27388-02041-1723https://doaj.org/article/3207bbe65e894dab9e6e7124d3c248492021-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27388-0https://doaj.org/toc/2041-1723Rearrangement hot spots (Rhs) proteins are bacterial polymorphic toxin systems. Here, the authors show that Rhs1 forms a complex with the Type VI secretion system (T6SS) spike protein VgrG and the EagR chaperone. They also present the cryo-EM structure of the Rhs1-EagR complex and propose a model for Rhs loading and delivery by the T6SS.Dukas JurėnasLeonardo Talachia RosaMartial ReyJulia Chamot-RookeRémi FronzesEric CascalesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Dukas Jurėnas
Leonardo Talachia Rosa
Martial Rey
Julia Chamot-Rooke
Rémi Fronzes
Eric Cascales
Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
description Rearrangement hot spots (Rhs) proteins are bacterial polymorphic toxin systems. Here, the authors show that Rhs1 forms a complex with the Type VI secretion system (T6SS) spike protein VgrG and the EagR chaperone. They also present the cryo-EM structure of the Rhs1-EagR complex and propose a model for Rhs loading and delivery by the T6SS.
format article
author Dukas Jurėnas
Leonardo Talachia Rosa
Martial Rey
Julia Chamot-Rooke
Rémi Fronzes
Eric Cascales
author_facet Dukas Jurėnas
Leonardo Talachia Rosa
Martial Rey
Julia Chamot-Rooke
Rémi Fronzes
Eric Cascales
author_sort Dukas Jurėnas
title Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
title_short Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
title_full Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
title_fullStr Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
title_full_unstemmed Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
title_sort mounting, structure and autocleavage of a type vi secretion-associated rhs polymorphic toxin
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/3207bbe65e894dab9e6e7124d3c24849
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