expression of glycosomal and mitochondrial proteins in the two major
life-cycle stages of Trypanosoma brucei.Mol
Biochem Parasitol. 2008 Apr;158(2):189-201. Epub 2007 Dec 23.
semi-quantitative differential three-dimensional liquid
chromatography coupled to mass spectrometry (3D-LC-MS/MS) was used
to compare the glycosomal and mitochondrial proteomes of the
bloodstream- and insect-form of Trypanosoma brucei. The abundance of
glycosomal marker proteins identified in the two life-cycle stages
corresponded well with the relative importance of biochemical
pathways present in the glycosomes of the two stages and the peptide
spectral count ratios of selected enzymes were in good agreement
with published data about their enzymatic specific activities. This
approach proved extremely useful for the generation of large scale
proteomics data for the comparison of different life-cycle stages.
Several proteins involved in oxidative stress protection,
sugar-nucleotide synthesis, purine salvage, nucleotide-monophosphate
formation and purine-nucleotide cycle were identified as glycosomal
The direct route:
a simplified pathway for protein import into the mitochondrion of
Cell Biol. 2008 Jan;18(1):12-8.
brucei is a unicellular eukaryote that causes the deadly human
African trypanosomiasis ('sleeping sickness') in humans. The
parasite has a complicated lifestyle, it developmentally changes
aspects of its mitochondrial function as it alternates from forms in
the tsetse fly to forms adapted for life in the human bloodstream.
The single mitochondrion found in each trypanosome has to be
duplicated precisely in each round of the cell cycle in order for
parasites to replicate, and this depends on the import of proteins
from the cytosol. Here we review what is known about the
mitochondrial protein import pathway in T. brucei, how it compares
with the process in humans, and how the distinguishing features seen
in T. brucei and humans promise new understanding of the
mitochondrial protein import process in all eukaryotes.