Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation
P in1‐type peptidyl‐prolyl cis/trans isomerases ( PPI ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a P in1‐type PPI ase in T rypanosoma cruzi , but little is known about its function and subcellular lo...
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Veröffentlicht in: | The Journal of eukaryotic microbiology 2013-01, Vol.60 (1), p.101-105 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | P
in1‐type peptidyl‐prolyl
cis/trans
isomerases (
PPI
ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a
P
in1‐type
PPI
ase in
T
rypanosoma cruzi
, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with
P
in1‐like proteins from diverse organisms,
Tc
P
in1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition,
RNAi
‐mediated downregulation of
Tb
P
in1 in
T
rypanosoma brucei
did not abolish cell proliferation. Using yeast two‐hybrid assay, we identified a
MORN
domain‐containing protein as putative
P
in1‐binding partners. These data suggest that
P
in1‐mediated signaling mechanism plays a different role in protozoan parasites. |
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ISSN: | 1066-5234 1550-7408 |
DOI: | 10.1111/jeu.12009 |