The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein

ATP-Binding Cassette transporters (ABC transporters) are protein complexes involved in the import and export of different molecules, including ions, sugars, peptides, drugs, and others. Due to the diversity of substrates, they have large relevance in physiological processes such as virulence, pathog...

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Autores principales:	Aline Sampaio Cremonesi, Lilia I. De la Torre, Maximillia Frazão de Souza, Gabriel S. Vignoli Muniz, M. Teresa Lamy, Cristiano Luis Pinto Oliveira, Andrea Balan
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Polyamine binding Substrate-binding protein PotF Xanthomonas citri Spermidine Putrescine Biology (General) QH301-705.5 Biochemistry QD415-436
Acceso en línea:	https://doaj.org/article/f89d508b49b94f3d821e82f16a7f8c37
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spelling	oai:doaj.org-article:f89d508b49b94f3d821e82f16a7f8c372021-11-18T04:50:30ZThe citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein2405-580810.1016/j.bbrep.2021.101171https://doaj.org/article/f89d508b49b94f3d821e82f16a7f8c372021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S240558082100265Xhttps://doaj.org/toc/2405-5808ATP-Binding Cassette transporters (ABC transporters) are protein complexes involved in the import and export of different molecules, including ions, sugars, peptides, drugs, and others. Due to the diversity of substrates, they have large relevance in physiological processes such as virulence, pathogenesis, and antimicrobial resistance. In Xanthomonas citri subsp. citri, the phytopathogen responsible for the citrus canker disease, 20% of ABC transporters components are expressed under infection conditions, including the putative putrescine/polyamine ABC transporter, PotFGHI. Polyamines are ubiquitous molecules that mediate cell growth and proliferation and play important role in bacterial infections. In this work, we characterized the X. citri periplasmic-binding protein PotF (XAC2476) using bioinformatics, biophysical and structural methods. PotF is highly conserved in Xanthomonas sp. genus, and we showed it is part of a set of proteins related to the import and assimilation of polyamines in X. citri. The interaction of PotF with putrescine and spermidine was direct and indirectly shown through fluorescence spectroscopy analyses, and experiments of circular dichroism (CD) and small-angle X-ray scattering (SAXS), respectively. The protein showed higher affinity for spermidine than putrescine, but both ligands induced structural changes that coincided with the closing of the domains and increasing of thermal stability.Aline Sampaio CremonesiLilia I. De la TorreMaximillia Frazão de SouzaGabriel S. Vignoli MunizM. Teresa LamyCristiano Luis Pinto OliveiraAndrea BalanElsevierarticlePolyamine bindingSubstrate-binding proteinPotFXanthomonas citriSpermidinePutrescineBiology (General)QH301-705.5BiochemistryQD415-436ENBiochemistry and Biophysics Reports, Vol 28, Iss , Pp 101171- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Polyamine binding Substrate-binding protein PotF Xanthomonas citri Spermidine Putrescine Biology (General) QH301-705.5 Biochemistry QD415-436
spellingShingle	Polyamine binding Substrate-binding protein PotF Xanthomonas citri Spermidine Putrescine Biology (General) QH301-705.5 Biochemistry QD415-436 Aline Sampaio Cremonesi Lilia I. De la Torre Maximillia Frazão de Souza Gabriel S. Vignoli Muniz M. Teresa Lamy Cristiano Luis Pinto Oliveira Andrea Balan The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
description	ATP-Binding Cassette transporters (ABC transporters) are protein complexes involved in the import and export of different molecules, including ions, sugars, peptides, drugs, and others. Due to the diversity of substrates, they have large relevance in physiological processes such as virulence, pathogenesis, and antimicrobial resistance. In Xanthomonas citri subsp. citri, the phytopathogen responsible for the citrus canker disease, 20% of ABC transporters components are expressed under infection conditions, including the putative putrescine/polyamine ABC transporter, PotFGHI. Polyamines are ubiquitous molecules that mediate cell growth and proliferation and play important role in bacterial infections. In this work, we characterized the X. citri periplasmic-binding protein PotF (XAC2476) using bioinformatics, biophysical and structural methods. PotF is highly conserved in Xanthomonas sp. genus, and we showed it is part of a set of proteins related to the import and assimilation of polyamines in X. citri. The interaction of PotF with putrescine and spermidine was direct and indirectly shown through fluorescence spectroscopy analyses, and experiments of circular dichroism (CD) and small-angle X-ray scattering (SAXS), respectively. The protein showed higher affinity for spermidine than putrescine, but both ligands induced structural changes that coincided with the closing of the domains and increasing of thermal stability.
format	article
author	Aline Sampaio Cremonesi Lilia I. De la Torre Maximillia Frazão de Souza Gabriel S. Vignoli Muniz M. Teresa Lamy Cristiano Luis Pinto Oliveira Andrea Balan
author_facet	Aline Sampaio Cremonesi Lilia I. De la Torre Maximillia Frazão de Souza Gabriel S. Vignoli Muniz M. Teresa Lamy Cristiano Luis Pinto Oliveira Andrea Balan
author_sort	Aline Sampaio Cremonesi
title	The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
title_short	The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
title_full	The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
title_fullStr	The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
title_full_unstemmed	The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein
title_sort	citrus plant pathogen xanthomonas citri has a dual polyamine-binding protein
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/f89d508b49b94f3d821e82f16a7f8c37
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The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein

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