IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Search and discovery of new enzymes working at low temperature belonging to Antarctic microorganisms.
Autor/es:
MARTÍN ARAN, LEONARDO PELLIZA, SEBASTIÁN KLINKE, JIMENA RINALDI, GASTÓN PARIS, CLARA SMAL, MARIANA GALLO, FERNANDO GOLDBAUM, DANIEL OSCAR CICERO.; ADRIÁN TURJANSKI, ; WALTER P. MAC CORMACK,; ANDRÉS BERCOVICH
Lugar:
Frauenchiemsee
Reunión:
Congreso; 35th FGMR Discussion Meeting and Joint Conference of the German, Italian and Slovenian Magnetic Resonance Societies Advanced Magnetic Resonance, Methods and Applications; 2013
Institución organizadora:
Italian and Slovenian Magnetic Resonance Societies Advanced Magnetic Resonance
Resumen:
Cold-adapted organisms and their enzymes offer a large variety of real and potential applications in different fields of biotechnology. Cold-adapted enzymes are characterized by a high catalytic efficiency at low and moderate temperatures. The discovery of new proteins with activity at low temperatures, and the comprehension of the molecular mechanisms open new perspective for industrial applications. In this context, the recently created Extremophiles Structural Genomics consortium (ESG), formed by the University of Rome, Tor Vergata, the University of Verona, Fundación Instituto Leloir (Argentina), the University of Buenos Aires and the Argentinean Antarctic Institute, has the aim of isolating and characterizing psychrophilic bacteria from Antarctic biotypes, for a subsequent search of proteins with enzymatic activity at low temperatures. As a starting point for this project, we undertook the analysis of proteins belonging to Bizionia argentinensis (BA), a newly discovered bacterium [1]. The genome of BA was recently decoded [2] and constitutes a relevant source for the discovery of new proteins. A particularly convenient protocol based on NMR experiments [3] was set up in order to identify the best candidates for structural determination. In this way, more than 30 proteins were classified as good candidates for three-dimensional structure determination. The hypothesis is that although the amino acidic sequence is not conserved, structural homology will allow the functional classification of the proteins and the discovery of new enzymes. We have already determined the structure of two proteins with unknown function belonging to BA: BA42 (by NMR) and C24 (by X-ray crystallography). In this presentation, the last results regarding the structural genomics project will be presented, as well as the first insights into the possible function of the two newly discovered proteins, BA42 and C24. References [1] Bercovich A. et al., International Journla of Systematic and Evolutionary Microbiology, 58, 2363-2367 (2008) [2] Lanzarotti E. et al., J. Bacteriol., 193, 6797-8 (2011) [3] Galvão-Botton, L.M.P., Katsuyama, A.M., Guzzo, C.R., Almedia, F.C.L., Farah, C.S. and Valente, A.P. FEBS Letters, 552, 207-213 (2003)