Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1803, Issue 9, Pages 1028-1037Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2010.05.006
Keywords
Peptidyl-prolyl cis/trans isomerase; Parvulin; Pin1-type PPIase; Par45
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Funding
- DAAD
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET, Argentina)
- Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT, Argentina)
- Prosul-CNPq
- FAPESP (Brazil)
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The parvulin family of peptidyl-prolyl cis/trans isomerases (PPIases) catalyzes the cis/trans isomerization of the peptide bonds preceding Pro residues. Eukaryotic parvulin-type PPIases have been shown to be involved in cell proliferation and cell cycle progression. Here we present the biochemical and molecular characterization of a novel multi-domain parvulin-type PPIase from the human pathogenic Trypanosoma cruzi, annotated as TcPar45. Like most other parvulins, Par45 has an N-terminal extension, but, in contrast to human Pin1, it contains a forkhead-associated domain (FHA) instead of a WW domain at the N-terminal end. Par45 shows a strong preference for a substrate with the basic Arg residue preceding Pro (Suc-Ala-Arg-Pro-Phe-NH-Np: k(cat)/K-M = 97.1 /M/s), like that found for human Part14. In contrast to human Pin1, but similarly to Par14, Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds. It is preferentially located in the parasite nucleus. Single RNA interference (RNAi)-mediated knock-down showed that there was a growth inhibition in procyclic Trypanosoma brucei cells. These results identify Par45 as a phosphorylation-independent parvulin required for normal cell proliferation in a unicellular eukaryotic cell. (C) 2010 Elsevier B.V. All rights reserved.
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