Functional characterization of two novel parvulins in Trypanosoma brucei |
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Authors: | Jian Yuan Goh Luuan Chin Tan Cynthia Y He Yih-Cherng Liou |
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Institution: | a NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore b Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore |
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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. |
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Keywords: | PPlase Peptidyl-prolyl isomerase FHA Pin1 Parvulin Trypanosoma brucei |
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