A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression. Here, we show that the novel type III effector XopL from t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Alexander U Singer, Sebastian Schulze, Tatiana Skarina, Xiaohui Xu, Hong Cui, Lennart Eschen-Lippold, Monique Egler, Tharan Srikumar, Brian Raught, Justin Lee, Dierk Scheel, Alexei Savchenko, Ulla Bonas
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4aad9687058448118ec2d3202dbc7729
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:4aad9687058448118ec2d3202dbc7729
record_format	dspace
spelling	oai:doaj.org-article:4aad9687058448118ec2d3202dbc77292021-11-18T06:06:07ZA pathogen type III effector with a novel E3 ubiquitin ligase architecture.1553-73661553-737410.1371/journal.ppat.1003121https://doaj.org/article/4aad9687058448118ec2d3202dbc77292013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23359647/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression. Here, we show that the novel type III effector XopL from the model plant pathogen Xanthomonas campestris pv. vesicatoria exhibits E3 ubiquitin ligase activity in vitro and in planta, induces plant cell death and subverts plant immunity. E3 ligase activity is associated with the C-terminal region of XopL, which specifically interacts with plant E2 ubiquitin conjugating enzymes and mediates formation of predominantly K11-linked polyubiquitin chains. The crystal structure of the XopL C-terminal domain revealed a single domain with a novel fold, termed XL-box, not present in any previously characterized E3 ligase. Mutation of amino acids in the central cavity of the XL-box disrupts E3 ligase activity and prevents XopL-induced plant cell death. The lack of cysteine residues in the XL-box suggests the absence of thioester-linked ubiquitin-E3 ligase intermediates and a non-catalytic mechanism for XopL-mediated ubiquitination. The crystal structure of the N-terminal region of XopL confirmed the presence of a leucine-rich repeat (LRR) domain, which may serve as a protein-protein interaction module for ubiquitination target recognition. While the E3 ligase activity is required to provoke plant cell death, suppression of PAMP responses solely depends on the N-terminal LRR domain. Taken together, the unique structural fold of the E3 ubiquitin ligase domain within the Xanthomonas XopL is unprecedented and highlights the variation in bacterial pathogen effectors mimicking this eukaryote-specific activity.Alexander U SingerSebastian SchulzeTatiana SkarinaXiaohui XuHong CuiLennart Eschen-LippoldMonique EglerTharan SrikumarBrian RaughtJustin LeeDierk ScheelAlexei SavchenkoUlla BonasPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 1, p e1003121 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Alexander U Singer Sebastian Schulze Tatiana Skarina Xiaohui Xu Hong Cui Lennart Eschen-Lippold Monique Egler Tharan Srikumar Brian Raught Justin Lee Dierk Scheel Alexei Savchenko Ulla Bonas A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
description	Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression. Here, we show that the novel type III effector XopL from the model plant pathogen Xanthomonas campestris pv. vesicatoria exhibits E3 ubiquitin ligase activity in vitro and in planta, induces plant cell death and subverts plant immunity. E3 ligase activity is associated with the C-terminal region of XopL, which specifically interacts with plant E2 ubiquitin conjugating enzymes and mediates formation of predominantly K11-linked polyubiquitin chains. The crystal structure of the XopL C-terminal domain revealed a single domain with a novel fold, termed XL-box, not present in any previously characterized E3 ligase. Mutation of amino acids in the central cavity of the XL-box disrupts E3 ligase activity and prevents XopL-induced plant cell death. The lack of cysteine residues in the XL-box suggests the absence of thioester-linked ubiquitin-E3 ligase intermediates and a non-catalytic mechanism for XopL-mediated ubiquitination. The crystal structure of the N-terminal region of XopL confirmed the presence of a leucine-rich repeat (LRR) domain, which may serve as a protein-protein interaction module for ubiquitination target recognition. While the E3 ligase activity is required to provoke plant cell death, suppression of PAMP responses solely depends on the N-terminal LRR domain. Taken together, the unique structural fold of the E3 ubiquitin ligase domain within the Xanthomonas XopL is unprecedented and highlights the variation in bacterial pathogen effectors mimicking this eukaryote-specific activity.
format	article
author	Alexander U Singer Sebastian Schulze Tatiana Skarina Xiaohui Xu Hong Cui Lennart Eschen-Lippold Monique Egler Tharan Srikumar Brian Raught Justin Lee Dierk Scheel Alexei Savchenko Ulla Bonas
author_facet	Alexander U Singer Sebastian Schulze Tatiana Skarina Xiaohui Xu Hong Cui Lennart Eschen-Lippold Monique Egler Tharan Srikumar Brian Raught Justin Lee Dierk Scheel Alexei Savchenko Ulla Bonas
author_sort	Alexander U Singer
title	A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
title_short	A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
title_full	A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
title_fullStr	A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
title_full_unstemmed	A pathogen type III effector with a novel E3 ubiquitin ligase architecture.
title_sort	pathogen type iii effector with a novel e3 ubiquitin ligase architecture.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/4aad9687058448118ec2d3202dbc7729
work_keys_str_mv	AT alexanderusinger apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT sebastianschulze apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT tatianaskarina apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT xiaohuixu apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT hongcui apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT lennarteschenlippold apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT moniqueegler apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT tharansrikumar apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT brianraught apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT justinlee apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT dierkscheel apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT alexeisavchenko apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT ullabonas apathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT alexanderusinger pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT sebastianschulze pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT tatianaskarina pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT xiaohuixu pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT hongcui pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT lennarteschenlippold pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT moniqueegler pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT tharansrikumar pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT brianraught pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT justinlee pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT dierkscheel pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT alexeisavchenko pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture AT ullabonas pathogentypeiiieffectorwithanovele3ubiquitinligasearchitecture
_version_	1718424535236083712

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

Ejemplares similares