Ontology highlight
ABSTRACT:
PROVIDER: PRJNA792722 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR17345015_1.fastq.gz | Fastqsanger.gz | |||
| SRR17345015_2.fastq.gz | Fastqsanger.gz | |||
| SRR17345016_subreads.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 3 of 3 |
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Project description:Study of kinetoplast genome and RNA editing of Trypanosoma lewisi
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Project description:The trypanosomatid flagellates possess in their single mitochondrion a highly complex kinetoplast (k) DNA, which is composed of interlocked circular molecules of two types. Dozens of maxicircles represent a classical mitochondrial genome, and thousands of minicircles encode guide (g)RNAs, which direct the processive and essential uridine insertion/deletion mRNA editing of maxicircle transcripts. While the details of kDNA structure and this type of RNA editing are well-established, our knowledge mostly relies on a narrow foray of intensely studied human parasites of the genera Leishmania and Trypanosoma. Here, we analyzed kDNA, its expression, and RNA editing of two members of the poorly characterized genus Vickermania with very different cultivation histories. In both Vickermania species, the gRNA-containing HL-circles are atypically large with multiple gRNAs each. Examination of V. spadyakhi HL-circle loci revealed a massive redundancy of gRNAs relative to the editing needs. In comparison, the HL-circle repertoire of extensively cultivated V. ingenoplastis is greatly reduced. It correlates with V. ingenoplastis-specific loss of productive editing of transcripts encoding subunits of respiratory chain complex I and corresponding lack of complex I activity. This loss in a parasite already lacking genes for subunits of complexes III and IV suggests an apparent requirement for its mitochondrial ATP synthase to work in reverse to maintain membrane potential. In contrast, V. spadyakhi retains a functional complex I that allows ATP synthase to work in its standard direction.
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Project description:Raw file submission for publication 'Poly(A) binding KPAF4/5 complex stabilizes kinetoplast mRNAs in Trypanosoma brucei'
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Project description:Mitochondrial DNA replication and gene expression are essential for cell survival. In Trypanosoma brucei, a protozoan animal and human parasite, the mitochondrial RNA polymerase (mtRNAP) plays roles in both transcription and DNA replication. This study identifies and characterizes the first mitochondrial transcription factor (mtTF1) in the Kinetoplastea. mtRNAP and mtTF1 form a high-molecular-weight complex that localizes to the kinetoplast DNA (kDNA) and is essential for parasite survival in both life cycle stages. Their localization is interdependent, and both proteins influence maxicircle replication, but not minicircle replication. Knockdown of either protein result in altered gene expression, particularly affecting the minor strand of the mitochondrial genome. Since mtTF1 is unique to the Kinetoplastea, it might prove to be a promising drug target.
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Project description:Structures of RNA editing substrate binding complexes reveal the mechanisms of guide RNA stabilization and messenger RNA recognition in the Trypanosoma brucei mitochondrion.
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Project description:Trypanosoma brucei requires extensive uridine insertion and deletion RNA editing of most of their mitochondrial transcripts to generate translatable open reading frames. The RNA editing substrate binding complex (RESC) serves as the scaffold that coordinates the protein-protein and protein-RNA interactions during editing. This project is to characterize the interactome of RESC6 and RESC8 protein by TurboID. Three replicates of each condition were performed.
2023-10-12 | PXD046097 | Pride
Project description:The kinetoplast is the large mitochondrial genome present in the eponymous Kinetoplastida. African trypanosomes can lose their kinetoplast DNA (kDNA), however, when the nuclear-encoded gamma subunit of the mitochondrial ATP-synthase (g-ATPase) is mutated. These mutations are also associated with multidrug resistance, tsetse-fly independent mechanical transmission, and geographical spread of these parasites beyond Africa. Here we engineer kinetoplast-independent kinetoplastids and explore origins and consequences of kDNA loss in Trypanosoma brucei. We used oligo targeting to edit the native g-ATPase gene, and selection with the ATP-synthase targeting drug oligomycin to enrich the desired mutants. Using this approach, we identified novel M282F, M282W, and M282Y mutants, and subsequently generated precision-edited strains expressing the M282F mutant or the previously described L262P or A273P mutants. These heterozygous mutants retained sensitivity to the kDNA-targeting drug acriflavine, however, and failed to yield kDNA negative cells following acriflavine selection. In contrast, T. brucei with a homozygous M282F edit were acriflavine resistant and readily tolerated acriflavine-induced kDNA loss. Proteomics analysis of the homozygous mutants revealed highly specific depletion of ATP synthase-associated proteins. Complete kDNA-loss in these cells was associated with substantial depletion of kDNA-binding proteins and mitochondrial RNA-processing factors. In contrast, mitochondrial membrane-associated transporters were increased in abundance. These results reveal g-ATPase defects that are analogous to a broken camshaft at the core of the ATP synthase rotary motor. In summary, T. brucei cells with a bi-allelic g-ATPase defect assemble a remodelled ATP synthase, and readily tolerate kDNA-loss, accompanied by substantial remodelling of the mitochondrial proteome.
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