IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Looking for enzymes under the ice of the Antarctic
Autor/es:
C. SMAL; E. LANZAROTTI; M. PAPOUCHADO; M. FORTI; M. ARAN; M. MARTI; M. GALLO; A. BERCOVICH; W.P. MAC CORMACK; A. TURJANSKY ; D. O. CICERO
Reunión:
Encuentro; Italian NMR Discussion Group; 2011
Resumen:
The genome of the bacteria Bizionia argentinensis, isolated from the Antarctic marine environment [1], was recently decoded and constitutes a relevant source for the discovery of new proteins showing biological activity in extreme conditions of low temperatures. These biomolecules can help the understanding of the general mechanisms that allow biological systems to adapt themselves to particular life conditions. In addition, they can be used in biotechnological applications that can benefit from the use of enzymes showing activity at low temperatures. As a part of the “White Genome” project in collaboration with Bio Sidus, a leading Biotech Argentinean company, the Bioinformatic Group at the University of Buenos Aires, and the Argentinean Antarctic Institute, we use Nuclear Magnetic Resonance (NMR) spectroscopy with a double purpose: i) to select a number of proteins with sequences that do not allow their functional classification, but that present characteristics of solubility and folding that make them good targets for structure determination, and ii) to determine the structure in solution of some of the targets previously selected. To this purpose we use a solid protocol already proved in a similar project dealing with proteins of Xanthomonas axonopodis pv. Citri [2]. In addition, comparison of proteins from this bacterium, living in extreme conditions, with corresponding analogs that work at higher temperature could shed light on the way proteins adapt their structure to very low temperature. As it is now recognized [3], most of the adaptation comes from an increased dynamics of the protein structure. For this reason, NMR represents the technique of choice to study these characteristics at atomic resolution. In this presentation, the first results of the protein selection process using bioinformatics tools, and the evaluation of the candidates using biochemical tools and NMR will be discussed.