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|Title:||Functional characterization of two novel parvulins in Trypanosoma brucei||Authors:||Goh, J.Y.
|Issue Date:||Jul-2010||Citation:||Goh, J.Y., Lai, C.-Y., Tan, L.C., Yang, D., He, C.Y., Liou, Y.-C. (2010-07). Functional characterization of two novel parvulins in Trypanosoma brucei. FEBS Letters 584 (13) : 2901-2908. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2010.04.077||Abstract:||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. © 2010 Federation of European Biochemical Societies.||Source Title:||FEBS Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/100721||ISSN:||00145793||DOI:||10.1016/j.febslet.2010.04.077|
|Appears in Collections:||Staff Publications|
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