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Article

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

Nature communications - 20 Apr 2020

Pei Tong-Tong, Li Hao, Liang Xiaoye, Wang Zeng-Hang, Liu Guangfeng, Wu Li-Li, Kim Haeun, Xie Zhiping, Yu Ming, Lin Shuangjun, Xu Ping, Dong Tao G

Abstract excerpt

Bacterial Rhs proteins containing toxic domains are often secreted by type VI secretion systems (T6SSs) through unclear mechanisms. Here, we show that the T6SS Rhs-family effector TseI of Aeromonas dhakensis is subject to self-cleavage at both the N- and the C-terminus, releasing the middle Rhs core and two VgrG-interacting domains (which we name VIRN and VIRC). VIRC is an endonuclease, and the immunity protein...

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Identifiers

PMID: 32313027
DOI: 10.1038/s41467-020-15774-z
PMCID: PMC7170923

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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