Structural basis for effector recognition by an antibacterial type IV secretion system.

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorOka, Gabriel Umaji-
Autor(es): dc.creatorSouza, Diorge Paulo de-
Autor(es): dc.creatorCenens, William-
Autor(es): dc.creatorMatsuyama, Bruno Yasui-
Autor(es): dc.creatorCardoso, Marcus Vinícius Cangussu-
Autor(es): dc.creatorOliveira, Luciana C.-
Autor(es): dc.creatorLima, Filipe da Silva-
Autor(es): dc.creatorCuccovia, Iolanda Midea-
Autor(es): dc.creatorCarvalho, Cristiane Rodrigues Guzzo-
Autor(es): dc.creatorSalinas, Roberto Kopke-
Autor(es): dc.creatorFarah, Shaker Chuck-
Data de aceite: dc.date.accessioned2025-08-21T15:32:06Z-
Data de disponibilização: dc.date.available2025-08-21T15:32:06Z-
Data de envio: dc.date.issued2023-05-23-
Data de envio: dc.date.issued2023-05-23-
Data de envio: dc.date.issued2021-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/jspui/handle/123456789/16647-
Fonte completa do material: dc.identifierhttps://doi.org/10.1073/pnas.2112529119-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1017667-
Descrição: dc.descriptionMany soil-, water-, and plant-associated bacterial species from the orders Xanthomonadales, Burkholderales, and Neisseriales carry a type IV secretion system (T4SS) specialized in translocating effec- tor proteins into other gram-negative species, leading to target cell death. These effectors, known as X-Tfes, carry a carboxyl- terminal domain of ∼120 residues, termed XVIPCD, characterized by several conserved motifs and a glutamine-rich tail. Previous studies showed that the XVIPCD is required for interaction with the T4SS coupling protein VirD4 and for T4SS-dependent translo- cation. However, the structural basis of the XVIPCD–VirD4 interac- tion is unknown. Here, we show that the XVIPCD interacts with the central all-alpha domain of VirD4 (VirD4AAD). We used solution NMR spectroscopy to solve the structure of the XVIPCD of X-TfeXAC2609 from Xanthomonas citri and to map its interaction surface with VirD4AAD. Isothermal titration calorimetry and in vivo Xanthomonas citri versus Escherichia coli competition assays using wild-type and mutant X-TfeXAC2609 and X-TfeXAC3634 indicate that XVIPCDs can be divided into two regions with distinct functions: the well-folded N-terminal region contains specific conserved motifs that are responsible for interactions with VirD4AAD, while both N- and carboxyl-terminal regions are required for effective X-Tfe translocation into the target cell. The conformational stabil- ity of the N-terminal region is reduced at and below pH 7.0, a prop- erty that may facilitate X-Tfe unfolding and translocation through the more acidic environment of the periplasm.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsaberto-
Direitos: dc.rightsThis article is distributed under Creative Commons Attribution-NonCommercialNoDerivatives License 4.0 (CC BY-NC-ND). Fonte: o PDF do artigo.-
Palavras-chave: dc.subjectBacterial competition-
Palavras-chave: dc.subjectProtein NMR-
Título: dc.titleStructural basis for effector recognition by an antibacterial type IV secretion system.-
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