Trypanosomatid pin1-type peptidyl-prolyl isomerase is cytosolic and not essential for cell proliferation
Esteban D Erben1, Sheila C Nardelli, Teresa C L de Jesus
1Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Hector N. Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, C1428ADN, Buenos Aires, R. Argentina. e.erben@zmbh.uni-heidelberg.de
Abstract:
Pin1-type peptidyl-prolyl cis/trans isomerases (PPIases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)-Pro residues, regulating various cellular events. Previously, we reported a Pin1-type PPIase in Trypanosoma cruzi, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with Pin1-like proteins from diverse organisms, TcPin1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition, RNAi-mediated downregulation of TbPin1 in Trypanosoma brucei did not abolish cell proliferation. Using yeast two-hybrid assay, we identified a MORN domain-containing protein as putative Pin1-binding partners. These data suggest that Pin1-mediated signaling mechanism plays a different role in protozoan parasites.
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