INGEBI   02650
INSTITUTO DE INVESTIGACIONES EN INGENIERIA GENETICA Y BIOLOGIA MOLECULAR "DR. HECTOR N TORRES"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
STUDY OF THE INTERACTION BETWEEN THE RIBOSOMAL STALK PROTEINS IN TRYPANOSOMA CRUZI
Autor/es:
SIMONETTI L., SMULSKI C.R., LONGHI S.A., JURI AYUB M., BASILE J.N., HOEBEKE J., LEVIN M.J.
Lugar:
Rosario, Santa Fé, Argentina
Reunión:
Congreso; VIII Congreso Argentino de Protozoología y Enfermedades Parasitarias; 2008
Institución organizadora:
Sociedad Argentina de Protozoologia
Resumen:
The stalk, in Trypanosoma cruzi, is composed by four proteins of about 11 KDa, TcP1a, TcP1b, TcP2a, TcP2b and a fifth TcP0 of about 30 KDa. These proteins play a critical role during the elongation step of protein synthesis
through interaction with elongation factor 2 (EF2). In order to study
the ribosomal P protein complex assembly, a yeast two-hybrid
interaction map was generated. Results showed a central role for TcP0.
Using Surface Plasmon Resonance the kinetics of each interaction
between the members of this protein family and with the EF2 were
analyzed. The assembly of ternary complexes was also assessed and the
interaction domains of TcP0 and TcP2b were mapped using truncated
proteins and synthetic peptides, respectively. Results indicated that
TcP0 and TcP2b proteins
were able to form homo dimers and also interact with both P1 and both
P2 proteins. Interaction with EF2 was observed for all P proteins, but
the low molecular weight P proteins showed a stronger affinity than
TcP0. The C-terminal region of TcP2b (peptide R15) seems to be involved
in the interaction with EF2, because R15 was able to inhibit the second
step of the association phase measured for the interaction of EF2 with
both TcP2a and TcP2b. Compared to other species, T. cruzi displays a specific pattern of ribosomal P protein interactions that could be targeted by selective therapeutic agents.