IDENTIFICATION OF PIN-TYPE PEPTIDYL-PROLYL ISOMERASE IN TRYPANOSOMA CRUZI

ERBEN E D; SCHIENE C; DAUM S; TÉLLEZ-IÑÓN M T

Glasgow, UK

Congreso; International Congress of Parasitology XI; 2006

Inernational Society of Parasitology

The peptidyl- prolyl cis/trans isomerases (PPIases) are a conserved family that catalyzes the cis/trans isomerization of the peptide bond precceding Proline residues. Prolyl isomerases include three major subfamilies: the cyclophilins, FK506 binding proteins and the parvulins. Recently, we have identified TcPin1 in Trypanosoma cruzi as a homologue of the parvulin hPin1 PPIase. The 117 amino acids of the TcPin1 display a 40% of identity with the catalytic core of hPin1 and is active as prolyl cis/trans isomerase. Furthermore, the substrate specificity of the recombinant TcPin1 indicates a preference for acidic residues NH2-terminal to proline. As all plants homologues identified, TcPin1 have not WW domain at the N‑terminus or analogous module. Nevertheless, TcPin1 is able to rescue the temperature‑sensitive phenotype of a mutation in the hPin1 homologue ESS1/PTF1 in S. cerevisiae. On the basis of functional assay and enzymatic PPIase activity w demonstrated that TcPin1 is a member of the Pin1‑type PPIases, suggesting the existence of an additional conserved level of post‑translational control in trypanosomatids.