Trypanosomatid pin1-type peptidyl-prolyl isomerase is cytosolic and not essential for cell proliferation.

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.

DOI: 10.1111/jeu.12009

Cite this paper

@article{Erben2013TrypanosomatidPP, title={Trypanosomatid pin1-type peptidyl-prolyl isomerase is cytosolic and not essential for cell proliferation.}, author={Esteban D. Erben and Sheila Cristina Nardelli and Teresa Cristina Leandro de Jesus and Sergio Schenkman and Mar{\'i}a Teresa T{\'e}llez-I{\~n}{\'o}n}, journal={The Journal of eukaryotic microbiology}, year={2013}, volume={60 1}, pages={101-5} }