THREE-DIMENSIONAL MODELS FOR Trypanosoma cruzi RIBOSOMAL STALK P PROTEINS

AMANTE ,ANALIA; GÓMEZ BARROZO JA; AGUILAR, CF

Mendoza

Congreso; XXXIV Reunión Científica Anual De La Sociedad De Biología De Cuyo; 2016

Sociedad De Biologia De Cuyo

Trypanosoma cruzi (T. cruzi) is the etiologic agent of the Chagas´ disease. The objective of our work is to study the threedimensionalstructure of T. cruzi ribosomal complex stalk in the large subunit of the ribosomes. The stalk is formed by the Pproteins: TcP0, TcP1, TcP1β, TcP2 and TcP2β. The TcP0 protein has 34 kDa, TcP1 and TcP2 proteins are smaller with amolecular weight of 10 kDa. The crystallographic structure of T. cruzi P0 and the stalk complex TcP0?TcP1α?TcP1β?TcP2α?TcP2β have not been solved to date. Previously, an homology model for TcP0 have been obtained in our laboratory. In this work,we have made three dimensional homology molecular models for these four proteins using the Modeller program. These proteinsare formed by three structural domains: an N-terminal α?domain, an inherently unstructured coiled A-rich domain and a Cterminalnegatively charged domain. The unstructured A-rich domain was characterized using several disorder predictors. Themolecular surface electrostatic potential and the hydrophobic surface were calculated. The surface properties are important for theC-terminal?s antigenic properties. We explored and identified protein interactions that may be involved in conformationalstability. This work represents the first three dimensional characterization for these T. cruzi proteins and provide clues forunderstand its functional properties.