Journal
FEBS LETTERS
Volume 584, Issue 13, Pages 2901-2908Publisher
WILEY
DOI: 10.1016/j.febslet.2010.04.077
Keywords
PPlase; Peptidyl-prolyl isomerase; FHA; Pin1; Parvulin; Trypanosoma brucei
Funding
- Biomedical Research Council [06/1/21/19/473]
- Agency for Science, Research and Technology, Singapore [R-154-000-403-112]
- Singapore NRF
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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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