Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris

Bacterial histidine kinases (HKs) play key roles in the response to stimuli and are regulated by reversible phosphorylation. Here, the authors show that the activity of a HK in the plant pathogen Xanthomonas campestris is modulated by irreversible, proteolytic modification in response to osmostress.

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Autores principales:	Chao-Ying Deng, Huan Zhang, Yao Wu, Li-Li Ding, Yue Pan, Shu-Tao Sun, Ya-Jun Li, Li Wang, Wei Qian
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bcc2da627214471c84d492da92fb8682
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spelling	oai:doaj.org-article:bcc2da627214471c84d492da92fb86822021-12-02T16:56:38ZProteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris10.1038/s41467-018-07228-42041-1723https://doaj.org/article/bcc2da627214471c84d492da92fb86822018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07228-4https://doaj.org/toc/2041-1723Bacterial histidine kinases (HKs) play key roles in the response to stimuli and are regulated by reversible phosphorylation. Here, the authors show that the activity of a HK in the plant pathogen Xanthomonas campestris is modulated by irreversible, proteolytic modification in response to osmostress.Chao-Ying DengHuan ZhangYao WuLi-Li DingYue PanShu-Tao SunYa-Jun LiLi WangWei QianNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Chao-Ying Deng Huan Zhang Yao Wu Li-Li Ding Yue Pan Shu-Tao Sun Ya-Jun Li Li Wang Wei Qian Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
description	Bacterial histidine kinases (HKs) play key roles in the response to stimuli and are regulated by reversible phosphorylation. Here, the authors show that the activity of a HK in the plant pathogen Xanthomonas campestris is modulated by irreversible, proteolytic modification in response to osmostress.
format	article
author	Chao-Ying Deng Huan Zhang Yao Wu Li-Li Ding Yue Pan Shu-Tao Sun Ya-Jun Li Li Wang Wei Qian
author_facet	Chao-Ying Deng Huan Zhang Yao Wu Li-Li Ding Yue Pan Shu-Tao Sun Ya-Jun Li Li Wang Wei Qian
author_sort	Chao-Ying Deng
title	Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
title_short	Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
title_full	Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
title_fullStr	Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
title_full_unstemmed	Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris
title_sort	proteolysis of histidine kinase vgrs inhibits its autophosphorylation and promotes osmostress resistance in xanthomonas campestris
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/bcc2da627214471c84d492da92fb8682
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Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris

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