3-methylcrotonyl Coenzyme A (CoA) carboxylase complex is involved in the Xanthomonas citri subsp. citri lifestyle during citrus infection

• Published in: PloS one Vol. 13; no. 6; p. e0198414
• Main Authors: Tomassetti, Mauro, Garavaglia, Betiana S, Vranych, Cecilia V, Gottig, Natalia, Ottado, Jorgelina, Gramajo, Hugo, Diacovich, Lautaro
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 07.06.2018; Public Library of Science (PLoS)
• Subjects: Amino acids; Analysis; Arabidopsis; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biocompatibility; Biofilms; Biology and Life Sciences; Biotin; Canker; Carbon-Carbon Ligases - genetics; Carbon-Carbon Ligases - metabolism; Carboxylases; Catabolism; Chain branching; Chains; Citrus - microbiology; Citrus canker; Cloning; Coenzyme A; Dehydrogenases; E coli; Enzymes; Escherichia coli; Fatty acids; Fitness; Gene mutation; Genes; Genetic aspects; Gram-negative bacteria; Host plants; Host-parasite relationships; Infections; Kinetics; Lesions; Leucine; Leucine - metabolism; Metabolism; Metabolites; Mutagenesis; Open Reading Frames - genetics; Physical Sciences; Plant diseases; Plant Diseases - microbiology; Protein Stability; Protein Subunits - genetics; Protein Subunits - metabolism; Proteins; Pseudomonas; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Risk factors; RNA polymerase; Substrate Specificity; Xanthomonas; Xanthomonas - enzymology; Xanthomonas - growth & development; Xanthomonas - physiology; Xanthomonas citri; Argentina
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0198414

Citrus canker is a disease caused by the phytopathogen Xanthomonas citri subsp. citri (Xcc), bacterium which is unable to survive out of the host for extended periods of time. Once established inside the plant, the pathogen must compete for resources and evade the defenses of the host cell. However, a number of aspects of Xcc metabolic and nutritional state, during the epiphytic stage and at different phases of infection, are poorly characterized. The 3-methylcrotonyl-CoA carboxylase complex (MCC) is an essential enzyme for the catabolism of the branched-chain amino acid leucine, which prevents the accumulation of toxic intermediaries, facilitates the generation of branched chain fatty acids and/or provides energy to the cell. The MCC complexes belong to a group of acyl-CoA carboxylases (ACCase) enzymes dependent of biotin. In this work, we have identified two ORFs (XAC0263 and XAC0264) encoding for the α and β subunits of an acyl-CoA carboxylase complex from Xanthomonas and demonstrated that this enzyme has MCC activity both in vitro and in vivo. We also found that this MCC complex is conserved in a group of pathogenic gram negative bacteria. The generation and analysis of an Xcc mutant strain deficient in MCC showed less canker lesions in the interaction with the host plant, suggesting that the expression of these proteins is necessary for Xcc fitness during infection.