Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system

Bacterial Rhs proteins with toxic domains are often secreted by type VI secretion systems. Here, the authors show that one of these proteins self-cleaves into three fragments, with the Rhs core and the N-terminal domain facilitating secretion and function of the C-terminal toxic domain.

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Autores principales:	Tong-Tong Pei, Hao Li, Xiaoye Liang, Zeng-Hang Wang, Guangfeng Liu, Li-Li Wu, Haeun Kim, Zhiping Xie, Ming Yu, Shuangjun Lin, Ping Xu, Tao G. Dong
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1410ae66c5d64cf8a5d2058c700ddb6e
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spelling	oai:doaj.org-article:1410ae66c5d64cf8a5d2058c700ddb6e2021-12-02T16:49:15ZIntramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system10.1038/s41467-020-15774-z2041-1723https://doaj.org/article/1410ae66c5d64cf8a5d2058c700ddb6e2020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15774-zhttps://doaj.org/toc/2041-1723Bacterial Rhs proteins with toxic domains are often secreted by type VI secretion systems. Here, the authors show that one of these proteins self-cleaves into three fragments, with the Rhs core and the N-terminal domain facilitating secretion and function of the C-terminal toxic domain.Tong-Tong PeiHao LiXiaoye LiangZeng-Hang WangGuangfeng LiuLi-Li WuHaeun KimZhiping XieMing YuShuangjun LinPing XuTao G. DongNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tong-Tong Pei Hao Li Xiaoye Liang Zeng-Hang Wang Guangfeng Liu Li-Li Wu Haeun Kim Zhiping Xie Ming Yu Shuangjun Lin Ping Xu Tao G. Dong Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
description	Bacterial Rhs proteins with toxic domains are often secreted by type VI secretion systems. Here, the authors show that one of these proteins self-cleaves into three fragments, with the Rhs core and the N-terminal domain facilitating secretion and function of the C-terminal toxic domain.
format	article
author	Tong-Tong Pei Hao Li Xiaoye Liang Zeng-Hang Wang Guangfeng Liu Li-Li Wu Haeun Kim Zhiping Xie Ming Yu Shuangjun Lin Ping Xu Tao G. Dong
author_facet	Tong-Tong Pei Hao Li Xiaoye Liang Zeng-Hang Wang Guangfeng Liu Li-Li Wu Haeun Kim Zhiping Xie Ming Yu Shuangjun Lin Ping Xu Tao G. Dong
author_sort	Tong-Tong Pei
title	Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
title_short	Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
title_full	Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
title_fullStr	Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
title_full_unstemmed	Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
title_sort	intramolecular chaperone-mediated secretion of an rhs effector toxin by a type vi secretion system
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/1410ae66c5d64cf8a5d2058c700ddb6e
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Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system

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