IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Characterization of an acyl-CoA carboxylase complex from Xanthomonas
Autor/es:
TOMASSETTI M; GARAVAGLIA B; GOTTIG N; OTTADO J; GRAMAJO H; DIACOVICH L
Lugar:
Rosario
Reunión:
Congreso; L Reunión Anual de la Sociedad Argentina de Investigación Bioquímica y Biología Molecular.; 2014
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB)
Resumen:
Phytopatogen Xanthomonas axonopodis pv. citri (Xac) produce canker, pathology that affects citric. Xac, as an obliged plant parasite, is unable to survive out of its host for long periods of time. Nevertheless, during the epiphytic survival state, over the leaf, many metabolic and nutritional aspects remain unknown. Branched-chain amino acid catabolism prevents their over-accumulation, facilitates branched-chain fatty acids biosynthesis and provides energy for the cell. The enzymatic complex 3-methyl-crotonyl-CoA carboxylase (MCC) is essential for leucine degradation pathway. MCC carboxylates its substrate, 3-methyl-crotonyl, to finally generate acetyl-CoA and acetoacetate which are latter incorporated into different metabolic pathways in case of nutritional stress or amino acid excess. complexes belong to the biotin-dependent acyl-CoA carboxylases (ACCases) group. We identified by bioinformatics two genes that may encode subunits of an ACCase complex in Xanthomonas, and others gram negative bacterial pathogens. The amino acidic sequences of these subunits present a high level of similarity to proteins of previously characterized MCC complexes from human and Pseudomonas aeruginosa. In this project we purified the MCC subunits and performed enzymatic activity assays using different acyl-CoAs as substrate. Now we propose to analyze the role of this complex in bacterial virulence.