2mnt

Publication Abstract from PubMed

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 Par14. 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.

Identification of an atypical peptidyl-prolyl cis/trans isomerase from trypanosomatids.,Erben ED, Valguarnera E, Nardelli S, Chung J, Daum S, Potenza M, Schenkman S, Tellez-Inon MT Biochim Biophys Acta. 2010 Sep;1803(9):1028-37. doi:, 10.1016/j.bbamcr.2010.05.006. Epub 2010 May 24. PMID:20580912^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.