INGEBI   02650
INSTITUTO DE INVESTIGACIONES EN INGENIERIA GENETICA Y BIOLOGIA MOLECULAR "DR. HECTOR N TORRES"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Searching the endogenous substrates of trypanosomatids parvulin-type prolyl peptidyl isomerases
Autor/es:
ERBEN E, VALGUARNERA E, POTENZA M AND TÉLLEZ-IÑÓN MT.
Lugar:
Ascochinga, Cordoba, Argentina
Reunión:
Jornada; XXIV Reunión Anual de la Sociedad Argentina de Protozoología; 2010
Institución organizadora:
SAP
Resumen:
In Trypanosma cruzi we have previously reported the characterization of three novel prolyl peptidyl isomerases (PPIases) belonging to the parvulins family, named TcPin1, TcPar14 and TcPar45. TcPin1, though lacking a conserved N-terminal WW domain, exhibits characteristic Pin1-like PPIase activity and can rescue the growth failure of ESS1-ts yeast mutant. On the other hand, TcPar45 acts preferentially on substrates containing the basic Arg residue preceding Pro and does not complement yeast Ess1 temperature-sensitive mutants. However, only depletion of this protein by RNAi, led to a marked slower procyclic T. brucei proliferation. Since FHA-domain containing proteins associate with numerous cellular processes including protein-protein interactions, transcriptional regulation, and DNA repair and degradation, the biological function of the FHA-domain containing parvulin, TcPar45, may increase our understanding how the parvulins work in a variety of cellular contexts. In addition, studies to identify specific substrates of the parvulins would provide a more comprehensive understanding of why conserved PPIases can have distinct isomerase specificities, and also enhance the existing knowledge of the biological functions of these enzymes. By using a proteomic approach and YTH analysis we found that Par45 associate with proteins involved in transcription and/or RNA processing. In this report, we propose a model to discuss the possible functional implications of these interactions. Supported with Foncyt and Conicet