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Functional characterization of two novel parvulins in Trypanosoma brucei
Author(s) -
Goh Jian Yuan,
Lai Cheng-Yu,
Tan Luuan Chin,
Yang Daiwen,
He Cynthia Y.,
Liou Yih-Cherng
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.077
Subject(s) - pin1 , trypanosoma brucei , isomerase , ww domain , mutant , biochemistry , saccharomyces cerevisiae , amino acid , biology , phosphorylation , yeast , prolyl isomerase , peptidylprolyl isomerase , chemistry , enzyme , gene
Parvulins belong to a family of peptidyl‐prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans conformations of prolyl‐peptidyl bonds. Herein, we characterized two novel parvulins, TbPIN1 and TbPAR42, in Trypanosoma brucei . TbPIN1, a 115 amino‐acid protein, contains a single PPIase domain but lacks the N‐terminal WW domain. Using NMR spectroscopy, TbPIN1 was found to exhibit PPIase activity toward a phosphorylated substrate. Overexpression of TbPIN1 can rescue the impaired temperature‐sensitive phenotype in a mutant yeast strain. TbPAR42, containing 383 amino acids, comprises a novel FHA domain at its N terminus and a C‐terminal PPIase domain but is a non‐Pin1‐type PPIase. Functionally, a knockdown of TbPAR42 in its procyclic form results in reduced proliferation rates suggesting an important role in cell growth.