ArticleEukaryotic cell2011
Three mitochondrial DNA polymerases are essential for kinetoplast DNA replication and survival of bloodstream form Trypanosoma brucei.
Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- A genome-wide genetic screen identifies a novel kDNA replication protein in trypanosomes.Nucleic acids research · 2026Article
- A trypanosome trifecta: an independently tunable triple inducible system for genetic studies inmSphere · 2026Article
- An independently tunable dual control system for RNAi complementation in Trypanosoma brucei.PloS one · 2025Article
- Identification of a conserved maxicircle and unique minicircles as part of the mitochondrial genome of Leishmania martiniquensis strain PCM3 in Thailand.Parasites & vectors · 2022Article
- Cytosolic and Mitochondrial Hsp90 in Cytokinesis, Mitochondrial DNA Replication, and Drug Action in Trypanosoma brucei.Antimicrobial agents and chemotherapy · 2021Article
- A DNA polymerization-independent role for mitochondrial DNA polymerase I-like protein C in African trypanosomes.Journal of cell science · 2020Article
- Inventory and Evolution of Mitochondrion-localized Family A DNA Polymerases in Euglenozoa.Pathogens (Basel, Switzerland) · 2020Article
- Cell cycle localization dynamics of mitochondrial DNA polymerase IC in African trypanosomes.Molecular biology of the cell · 2018Article
- Characterization of the novel mitochondrial genome replication factor MiRF172 inJournal of cell science · 2018Article
- A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei.PLoS pathogens · 2017Article
- A putative Leishmania DNA polymerase theta protects the parasite against oxidative damage.Nucleic acids research · 2016Article
- Trypanocidal action of bisphosphonium salts through a mitochondrial target in bloodstream form Trypanosoma brucei.International journal for parasitology. Drugs and drug resistance · 2016Article
- U-insertion/deletion RNA editing multiprotein complexes and mitochondrial ribosomes in Leishmania tarentolae are located in antipodal nodes adjacent to the kinetoplast DNA.Mitochondrion · 2015Article
- Article
- Independence from Kinetoplast DNA maintenance and expression is associated with multidrug resistance in Trypanosoma brucei in vitro.Antimicrobial agents and chemotherapy · 2014Article
- Trypanosoma brucei Tb927.2.6100 is an essential protein associated with kinetoplast DNA.Eukaryotic cell · 2013Article
- Dual functions of α-ketoglutarate dehydrogenase E2 in the Krebs cycle and mitochondrial DNA inheritance in Trypanosoma brucei.Eukaryotic cell · 2013Article
- Dynamic localization of Trypanosoma brucei mitochondrial DNA polymerase ID.Eukaryotic cell · 2012Article
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3 authors.
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Abstract
Trypanosoma brucei, the causative agent of human African trypanosomiasis, has a complex life cycle that includes multiple life cycle stages and metabolic changes as the parasite switches between insect vector and mammalian host. The parasite's single mitochondrion contains a unique catenated mitochondrial DNA network called kinetoplast DNA (kDNA) that is composed of minicircles and maxicircles. Long-standing uncertainty about the requirement of kDNA in bloodstream form (BF) T. brucei has recently eroded, with reports of posttranscriptional editing and subsequent translation of kDNA-encoded transcripts as essential processes for BF parasites. These studies suggest that kDNA and its faithful replication are indispensable for this life cycle stage. Here we demonstrate that three kDNA replication proteins (mitochondrial DNA polymerases IB, IC, and ID) are required for BF parasite viability. Silencing of each polymerase was lethal, resulting in kDNA loss, persistence of prereplication DNA monomers, and collapse of the mitochondrial membrane potential. These data demonstrate that kDNA replication is indeed crucial for BF T. brucei. The contributions of mitochondrial DNA polymerases IB, IC, and ID to BF parasite viability suggest that these and other kDNA replication proteins warrant further investigation as a new class of targets for the development of antitrypanosomal drugs.
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