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https://doi.org/10.1016/j.febslet.2010.04.077
| Title: | Functional characterization of two novel parvulins in Trypanosoma brucei | Authors: | Goh, J.Y. Lai, C.-Y. Tan, L.C. Yang, D. He, C.Y. Liou, Y.-C. |
Keywords: | FHA Parvulin Peptidyl-prolyl isomerase Pin1 PPlase Trypanosoma brucei |
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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