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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| Format: | Article |
| Language: | English |
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Elsevier
2021-12-01
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| Series: | Biochemistry and Biophysics Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S240558082100265X |
| _version_ | 1819177718451798016 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-22T21:31:07Z |
| format | Article |
| id | doaj.art-f89d508b49b94f3d821e82f16a7f8c37 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-22T21:31:07Z |
| publishDate | 2021-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-f89d508b49b94f3d821e82f16a7f8c372022-12-21T18:11:55ZengElsevierBiochemistry and Biophysics Reports2405-58082021-12-0128101171The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding proteinAline Sampaio Cremonesi0Lilia I. De la Torre1Maximillia Frazão de Souza2Gabriel S. Vignoli Muniz3M. Teresa Lamy4Cristiano Luis Pinto Oliveira5Andrea Balan6Programa de Pós-graduação Interunidades em Biotecnologia, Universidade de São Paulo, 05508-900, SP, Brazil; Laboratório de Biologia Estrutural Aplicada LBEA, Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, 05508-900, SP, BrazilLaboratório de Biologia Estrutural Aplicada LBEA, Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, 05508-900, SP, Brazil; Programa de Pós-graduação em Genética e Biología Molecular, Universidade Estadual de Campinas, 13083 – 970, SP, Brazil; Grupo Investigaciones Biomédicas, Departamento de Biología y Química, Universidad de Sucre, 700003, Sucre, ColombiaGrupo de Fluidos Complexos, Departamento de Física Experimental, Instituto de Física, Universidade de São Paulo, 05508-090, SP, BrazilLaborátorio de Biomembranas, Instituto de Física, Universidade de São Paulo, 05508-090, SP, BrazilLaborátorio de Biomembranas, Instituto de Física, Universidade de São Paulo, 05508-090, SP, BrazilGrupo de Fluidos Complexos, Departamento de Física Experimental, Instituto de Física, Universidade de São Paulo, 05508-090, SP, BrazilLaboratório de Biologia Estrutural Aplicada LBEA, Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, 05508-900, SP, Brazil; Corresponding author.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.http://www.sciencedirect.com/science/article/pii/S240558082100265XPolyamine bindingSubstrate-binding proteinPotFXanthomonas citriSpermidinePutrescine |
| spellingShingle | 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 Biochemistry and Biophysics Reports Polyamine binding Substrate-binding protein PotF Xanthomonas citri Spermidine Putrescine |
| title | 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_short | 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 |
| topic | Polyamine binding Substrate-binding protein PotF Xanthomonas citri Spermidine Putrescine |
| url | http://www.sciencedirect.com/science/article/pii/S240558082100265X |
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