Please use this identifier to cite or link to this item: 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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

8
checked on Oct 16, 2019

WEB OF SCIENCETM
Citations

8
checked on Oct 16, 2019

Page view(s)

44
checked on Oct 12, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.