Journal
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 171, Issue 1, Pages 45-49Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2010.01.002
Keywords
Trypanosoma brucei; Metabolic compartmentalization; Glycosome; Peroxisome; Glycosome-targeting; Triosephosphate isomerase
Categories
Funding
- 'Fonds de la Recherche Scientific Medicale' (Belgium)
- 'Fonds pour la Formation a la Recherche dans l'Industrie et l'Agriculture' (Belgium)
Ask authors/readers for more resources
In kinetoplastid protists, glycolysis is compartmentalized in glycosomes, organelles belonging to the peroxisome family. The Trypanosoma brucei glycosomal enzyme triosephosphate isomerase (TPI) does not contain either of the two established peroxisome-targeting signals, but we identified a 22 amino acids long fragment, present at an internal position of the polypeptide, that has the capacity to route a reporter protein to glycosomes in transfected trypanosomes, as demonstrated by cell-fractionation experiments and corroborating immunofluorescence studies. This polypeptide-internal routing information seems to be unique for the sequence of the trypanosome enzyme: a reporter protein fused to a Saccharomyces cerevisiae peptide containing the sequence corresponding to the 22-residue fragment of the T. brucei enzyme, was not targeted to glycosomes. In yeasts, as in most other organisms, TPI is indeed exclusively present in the cytosol. These results suggest that it may be possible to develop new trypanocidal drugs by targeting specifically the glycosome import mechanism of TPI. (C) 2010 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available