Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.

The type VI secretion system (T6SS) is a widespread protein secretion system found in many Gram-negative bacteria. T6SSs are highly regulated by various regulatory systems at multiple levels, including post-translational regulation via threonine (Thr) phosphorylation. The Ser/Thr protein kinase PpkA...

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Autores principales:	Jer-Sheng Lin, Hsin-Hui Wu, Pang-Hung Hsu, Lay-Sun Ma, Yin-Yuin Pang, Ming-Daw Tsai, Erh-Min Lai
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/88379400d80b47b285da98700c62bfc1
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spelling	oai:doaj.org-article:88379400d80b47b285da98700c62bfc12021-11-18T06:06:51ZFha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.1553-73661553-737410.1371/journal.ppat.1003991https://doaj.org/article/88379400d80b47b285da98700c62bfc12014-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24626341/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The type VI secretion system (T6SS) is a widespread protein secretion system found in many Gram-negative bacteria. T6SSs are highly regulated by various regulatory systems at multiple levels, including post-translational regulation via threonine (Thr) phosphorylation. The Ser/Thr protein kinase PpkA is responsible for this Thr phosphorylation regulation, and the forkhead-associated (FHA) domain-containing Fha-family protein is the sole T6SS phosphorylation substrate identified to date. Here we discovered that TssL, the T6SS inner-membrane core component, is phosphorylated and the phosphorylated TssL (p-TssL) activates type VI subassembly and secretion in a plant pathogenic bacterium, Agrobacterium tumefaciens. Combining genetic and biochemical approaches, we demonstrate that TssL is phosphorylated at Thr 14 in a PpkA-dependent manner. Further analysis revealed that the PpkA kinase activity is responsible for the Thr 14 phosphorylation, which is critical for the secretion of the T6SS hallmark protein Hcp and the putative toxin effector Atu4347. TssL phosphorylation is not required for the formation of the TssM-TssL inner-membrane complex but is critical for TssM conformational change and binding to Hcp and Atu4347. Importantly, Fha specifically interacts with phosphothreonine of TssL via its pThr-binding motif in vivo and in vitro and this interaction is crucial for TssL interaction with Hcp and Atu4347 and activation of type VI secretion. In contrast, pThr-binding ability of Fha is dispensable for TssM structural transition. In conclusion, we discover a novel Thr phosphorylation event, in which PpkA phosphorylates TssL to activate type VI secretion via its direct binding to Fha in A. tumefaciens. A model depicting an ordered TssL phosphorylation-induced T6SS assembly pathway is proposed.Jer-Sheng LinHsin-Hui WuPang-Hung HsuLay-Sun MaYin-Yuin PangMing-Daw TsaiErh-Min LaiPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 10, Iss 3, p e1003991 (2014)
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 Jer-Sheng Lin Hsin-Hui Wu Pang-Hung Hsu Lay-Sun Ma Yin-Yuin Pang Ming-Daw Tsai Erh-Min Lai Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
description	The type VI secretion system (T6SS) is a widespread protein secretion system found in many Gram-negative bacteria. T6SSs are highly regulated by various regulatory systems at multiple levels, including post-translational regulation via threonine (Thr) phosphorylation. The Ser/Thr protein kinase PpkA is responsible for this Thr phosphorylation regulation, and the forkhead-associated (FHA) domain-containing Fha-family protein is the sole T6SS phosphorylation substrate identified to date. Here we discovered that TssL, the T6SS inner-membrane core component, is phosphorylated and the phosphorylated TssL (p-TssL) activates type VI subassembly and secretion in a plant pathogenic bacterium, Agrobacterium tumefaciens. Combining genetic and biochemical approaches, we demonstrate that TssL is phosphorylated at Thr 14 in a PpkA-dependent manner. Further analysis revealed that the PpkA kinase activity is responsible for the Thr 14 phosphorylation, which is critical for the secretion of the T6SS hallmark protein Hcp and the putative toxin effector Atu4347. TssL phosphorylation is not required for the formation of the TssM-TssL inner-membrane complex but is critical for TssM conformational change and binding to Hcp and Atu4347. Importantly, Fha specifically interacts with phosphothreonine of TssL via its pThr-binding motif in vivo and in vitro and this interaction is crucial for TssL interaction with Hcp and Atu4347 and activation of type VI secretion. In contrast, pThr-binding ability of Fha is dispensable for TssM structural transition. In conclusion, we discover a novel Thr phosphorylation event, in which PpkA phosphorylates TssL to activate type VI secretion via its direct binding to Fha in A. tumefaciens. A model depicting an ordered TssL phosphorylation-induced T6SS assembly pathway is proposed.
format	article
author	Jer-Sheng Lin Hsin-Hui Wu Pang-Hung Hsu Lay-Sun Ma Yin-Yuin Pang Ming-Daw Tsai Erh-Min Lai
author_facet	Jer-Sheng Lin Hsin-Hui Wu Pang-Hung Hsu Lay-Sun Ma Yin-Yuin Pang Ming-Daw Tsai Erh-Min Lai
author_sort	Jer-Sheng Lin
title	Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
title_short	Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
title_full	Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
title_fullStr	Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
title_full_unstemmed	Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.
title_sort	fha interaction with phosphothreonine of tssl activates type vi secretion in agrobacterium tumefaciens.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/88379400d80b47b285da98700c62bfc1
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Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens.

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