UNIQUE STRUCTURAL AND FUNCTIONAL FEATURES OF TRYPANOSOMA CRUZI RIBOSOMES AS DETECTED BY YEAST TWO-HYBRID, SEQUENCE COMPARISON AND CRYO-ELECTRON MICROSCOPY

MAXIMILIANO JURI AYUB; HAIXIAO GAO; BENSON NYAMBEGA; SEBASTIÁN TANCO; JOACHIM FRANK; MARIANO LEVIN

Iguazú, Misiones, Argentina

Congreso; XL Reunión Anual Sociedad Argentina de Investigación Bioquímica y Biología Molecular; 2004

Sociedad Argentina de Investigación Bioquímica

Ribosomal P proteins form a conserved ribosomal structure, named the stalk, involved in the translocation step of protein synthesis. T. cruzi P proteins were initially cloned as major antigens recognized by the host immune system during the chronic phase of Chagas Disease. Sequencing of these proteins revealed specific features of the T. cruzi P protein system. The complete set of T. cruzi P proteins was cloned and studied using yeast two-hybrid. Comparison with yeast and mammals reveals a parasite-specific profile of protein interactions. Together with this, analysis of rRNA and protein ribosomal genes obtained from the T. cruzi genome databank show several parasite specific signatures. In order to confirm these observations, we used cryo-electron microscopy (CEM) to reconstruct the T. cruzi ribosome at 12.6 Å resolution. Notably, remarkable and unique features of the parasite ribosome correlate with experimental and data mining findings.