The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.

Type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria that undergo cycles of extension and retraction and participate in a variety of important functions related to lifestyle, defense and pathogenesis. During pilus extensions, the PilB ATPa...

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Autores principales:	Edgar E Llontop, William Cenens, Denize C Favaro, Germán G Sgro, Roberto K Salinas, Cristiane R Guzzo, Chuck S Farah
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/467fff9ee41f4dbcabb539a590b31955
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spelling	oai:doaj.org-article:467fff9ee41f4dbcabb539a590b319552021-12-02T20:00:23ZThe PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.1553-73661553-737410.1371/journal.ppat.1009808https://doaj.org/article/467fff9ee41f4dbcabb539a590b319552021-08-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009808https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria that undergo cycles of extension and retraction and participate in a variety of important functions related to lifestyle, defense and pathogenesis. During pilus extensions, the PilB ATPase energizes the polymerization of pilin monomers from the inner membrane. In Xanthomonas citri, two cytosolic proteins, PilZ and the c-di-GMP receptor FimX, are involved in the regulation of T4P biogenesis through interactions with PilB. In vivo fluorescence microscopy studies show that PilB, PilZ and FimX all colocalize to the leading poles of X. citri cells during twitching motility and that this colocalization is dependent on the presence of all three proteins. We demonstrate that full-length PilB, PilZ and FimX can interact to form a stable complex as can PilB N-terminal, PilZ and FimX C-terminal fragments. We present the crystal structures of two binary complexes: i) that of the PilB N-terminal domain, encompassing sub-domains ND0 and ND1, bound to PilZ and ii) PilZ bound to the FimX EAL domain within a larger fragment containing both GGDEF and EAL domains. Evaluation of PilZ interactions with PilB and the FimX EAL domain in these and previously published structures, in conjunction with mutagenesis studies and functional assays, allow us to propose an internally consistent model for the PilB-PilZ-FimX complex and its interactions with the PilM-PilN complex in the context of the inner membrane platform of the X. citri Type IV pilus.Edgar E LlontopWilliam CenensDenize C FavaroGermán G SgroRoberto K SalinasCristiane R GuzzoChuck S FarahPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 8, p e1009808 (2021)
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 Edgar E Llontop William Cenens Denize C Favaro Germán G Sgro Roberto K Salinas Cristiane R Guzzo Chuck S Farah The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
description	Type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria that undergo cycles of extension and retraction and participate in a variety of important functions related to lifestyle, defense and pathogenesis. During pilus extensions, the PilB ATPase energizes the polymerization of pilin monomers from the inner membrane. In Xanthomonas citri, two cytosolic proteins, PilZ and the c-di-GMP receptor FimX, are involved in the regulation of T4P biogenesis through interactions with PilB. In vivo fluorescence microscopy studies show that PilB, PilZ and FimX all colocalize to the leading poles of X. citri cells during twitching motility and that this colocalization is dependent on the presence of all three proteins. We demonstrate that full-length PilB, PilZ and FimX can interact to form a stable complex as can PilB N-terminal, PilZ and FimX C-terminal fragments. We present the crystal structures of two binary complexes: i) that of the PilB N-terminal domain, encompassing sub-domains ND0 and ND1, bound to PilZ and ii) PilZ bound to the FimX EAL domain within a larger fragment containing both GGDEF and EAL domains. Evaluation of PilZ interactions with PilB and the FimX EAL domain in these and previously published structures, in conjunction with mutagenesis studies and functional assays, allow us to propose an internally consistent model for the PilB-PilZ-FimX complex and its interactions with the PilM-PilN complex in the context of the inner membrane platform of the X. citri Type IV pilus.
format	article
author	Edgar E Llontop William Cenens Denize C Favaro Germán G Sgro Roberto K Salinas Cristiane R Guzzo Chuck S Farah
author_facet	Edgar E Llontop William Cenens Denize C Favaro Germán G Sgro Roberto K Salinas Cristiane R Guzzo Chuck S Farah
author_sort	Edgar E Llontop
title	The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
title_short	The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
title_full	The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
title_fullStr	The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
title_full_unstemmed	The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.
title_sort	pilb-pilz-fimx regulatory complex of the type iv pilus from xanthomonas citri.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/467fff9ee41f4dbcabb539a590b31955
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The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.

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