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

• Published in: Biochemistry and biophysics reports Vol. 28; p. 101171
• Main Authors: Cremonesi, Aline Sampaio, De la Torre, Lilia I., Frazão de Souza, Maximillia, Vignoli Muniz, Gabriel S., Lamy, M. Teresa, Pinto Oliveira, Cristiano Luis, Balan, Andrea
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2021; Elsevier
• Subjects: Ligand-induced conformational changes; Polyamine binding; PotF; Putrescine; Spermidine; Substrate-binding protein; Xanthomonas citri; Ligand-induced conformational changes; Xanthomonas citri; Substrate-binding protein; Spermidine; PotF; Putrescine; Polyamine binding
• ISSN: 2405-5808; 2405-5808
• DOI: 10.1016/j.bbrep.2021.101171

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.