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Trypanosomatid Pin1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation
Authors:Esteban D Erben  Sheila C Nardelli  Teresa C L de Jesus  Sergio Schenkman  Maria T Tellez‐Iñon
Institution:1. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Hector N. Torres” (INGEBI‐CONICET), , C1428ADN Buenos Aires, R. Argentina;2. Departamento de Microbiologia, Imunologia e Parasitologia, Universidade Federal de S?o Paulo, , 04023‐062 S?o Paulo, Brazil
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.
Keywords:MORN domain  parvulin  peptidyl‐prolyl isomerase  Pin1  PPIase     Trypanosoma cruzi   
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