Structural highlights
Publication Abstract from PubMed
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.
Functional characterization of two novel parvulins in Trypanosoma brucei.,Goh JY, Lai CY, Tan LC, Yang D, He CY, Liou YC FEBS Lett. 2010 Jul 2;584(13):2901-8. doi: 10.1016/j.febslet.2010.04.077. Epub, 2010 May 11. PMID:20466001[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goh JY, Lai CY, Tan LC, Yang D, He CY, Liou YC. Functional characterization of two novel parvulins in Trypanosoma brucei. FEBS Lett. 2010 Jul 2;584(13):2901-8. doi: 10.1016/j.febslet.2010.04.077. Epub, 2010 May 11. PMID:20466001 doi:http://dx.doi.org/10.1016/j.febslet.2010.04.077
