Trypanosomatid Pin1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation |
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Authors: | Esteban D Erben Sheila C Nardelli Teresa C L de Jesus Sergio Schenkman Maria T Tellez‐Iñon |
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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 |
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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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Keywords: | MORN domain parvulin peptidyl‐prolyl isomerase Pin1 PPIase
Trypanosoma cruzi
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