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A Quantitative Spatial Proteomics Analysis of Proteome Turnover in Human Cells*
TLDR
A subset of proteins was identified that exist in pools with different turnover rates depending on their subcellular localization, suggesting a general mechanism whereby their assembly is controlled in a different sub cellular location to their main site of function. Expand
The single mitochondrial porin of Trypanosoma brucei is the main metabolite transporter in the outer mitochondrial membrane.
TLDR
Results demonstrate that the mitochondria isolated from homozygous knockout cells did not produce adenosine-triphosphate in response to added substrates, but ATP production was restored by physical disruption of the outer membrane, demonstrating that the mitochondrial porin identified in T. brucei is the main metabolite channel in the outer membranes and therefore the functional orthologue of VDAC. Expand
Dual targeting of a single tRNA(Trp) requires two different tryptophanyl-tRNA synthetases in Trypanosoma brucei.
TLDR
RNA interference analysis established that both Trp RS1 and TrpRS2 are essential for growth and required for cytosolic and mitochondrial tryptophanyl-tRNA formation, respectively, and the notion that, in an organism, all nuclear-encoded tRNAs assigned to a given amino acid are charged by a single aminoacyl-t RNA synthetase is not universally valid. Expand
Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space.
TLDR
It is shown that no "Tim12" family of proteins exist, but rather that variant forms of the cognate small TIMs have been recently duplicated and modified to provide new functions: the yeast Tim12 is a modified form of Tim10, whereas in humans and some protists variant formsof Tim9, Tim8, and Tim13 are found instead. Expand
In vivo study in Trypanosoma brucei links mitochondrial transfer RNA import to mitochondrial protein import
TLDR
Ablation of Tim17 and mitochondrial heat‐shock protein 70, components of the inner‐membrane protein translocation machinery, strongly inhibits import of newly synthesized tRNAs, suggesting that the requirement for mitochondrial protein‐import factors might be a conserved feature of mitochondrial tRNA import in all systems. Expand
Mitochondrial Initiation Factor 2 of Trypanosoma brucei Binds Imported Formylated Elongator-type tRNAMet*
TLDR
The present study has identified initiation factor 2 of T. brucei and shown that its carboxyl-terminal domain specifically binds formylated trypanosomal elongator tRNAMet, suggesting that the main determinant recognized is theformylated methionine. Expand
Elongation factor 1a mediates the specificity of mitochondrial tRNA import in T. brucei
TLDR
It is shown that ablation of cytosolic eEF1a, but not of initiation factor 2, inhibits mitochondrial import of newly synthesized tRNAs well before translation or growth is affected. Expand
Dual Targeting of a tRNAAsp Requires Two Different Aspartyl-tRNA Synthetases in Trypanosoma brucei*
TLDR
Mitochondrial Tb-AspRS2 defines a novel group of eukaryotic AspRSs with an expanded substrate specificity that are restricted to trypanosomatids and therefore may be exploited as a novel drug target. Expand
Isolation of mitochondria from procyclic Trypanosoma brucei.
TLDR
The two most commonly used methods to isolate mitochondria from insect stage T. brucei are described and discussed. Expand
Trypanosoma Seryl-tRNA Synthetase Is a Metazoan-like Enzyme with High Affinity for tRNASec*
Trypanosomatids are important human pathogens that form a basal branch of eukaryotes. Their evolutionary history is still unclear as are many aspects of their molecular biology. Here we characterizeExpand
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