ArticleMolecular biology of the cell2003
A high-order trans-membrane structural linkage is responsible for mitochondrial genome positioning and segregation by flagellar basal bodies in trypanosomes.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
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Who cites it
130 citing papers in PubMed.
- A genome-wide genetic screen identifies a novel kDNA replication protein in trypanosomes.Nucleic acids research · 2026Article
- The segregation of organelles and organellar genomes across eukaryotic biology.Biochemical Society transactions · 2026Review
- Why Euglenozoans.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The subcellular architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Connecting basal body and mitochondrial DNA: TAC53 and the tubular organization of the tripartite attachment complex.PLoS pathogens · 2025Article
- Assembly of the mitochondrial outer membrane module of the trypanosomal tripartite attachment complex.PLoS pathogens · 2025Article
- From mitochondrial DNA arrangement to repair: a kinetoplast-associated protein with different roles in two trypanosomatid species.Parasites & vectors · 2025Article
- An independently tunable dual control system for RNAi complementation in Trypanosoma brucei.PloS one · 2025Article
- Molecular characterization of the permanent outer-inner membrane contact site of the mitochondrial genome segregation complex in trypanosomes.PLoS pathogens · 2024Article
- Pam16 and Pam18 were repurposed during Trypanosoma brucei evolution to regulate the replication of mitochondrial DNA.PLoS biology · 2024Article
- Biogenesis, inheritance, and 3D ultrastructure of the microsporidian mitosome.Life science alliance · 2024Article
- Mitochondrial genome maintenance-the kinetoplast story.FEMS microbiology reviews · 2023Review
- FAZ assembly in bloodstream formMolecular biology of the cell · 2023Article
- Characterization of two novel proteins involved in mitochondrial DNA anchoring in Trypanosoma brucei.PLoS pathogens · 2023Article
- Single p197 molecules of the mitochondrial genome segregation system ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- p166 links membrane and intramitochondrial modules of the trypanosomal tripartite attachment complex.PLoS pathogens · 2022Article
- Activity of alkaloids from Aspidosperma nitidum against Leishmania (Leishmania) amazonensis.Scientific reports · 2022Article
- Inheritance of the reduced mitochondria of Giardia intestinalis is coupled to the flagellar maturation cycle.BMC biology · 2021Article
- Article
70 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
In trypanosomes, the large mitochondrial genome within the kinetoplast is physically connected to the flagellar basal bodies and is segregated by them during cell growth. The structural linkage enabling these phenomena is unknown. We have developed novel extraction/fixation protocols to characterize the links involved in kinetoplast-flagellum attachment and segregation. We show that three specific components comprise a structure that we have termed the tripartite attachment complex (TAC). The TAC involves a set of filaments linking the basal bodies to a zone of differentiated outer and inner mitochondrial membranes and a further set of intramitochondrial filaments linking the inner face of the differentiated membrane zone to the kinetoplast. The TAC and flagellum-kinetoplast DNA connections are sustained throughout the cell cycle and are replicated and remodeled during the periodic kinetoplast DNA S phase. This understanding of the high-order trans-membrane linkage provides an explanation for the spatial position of the trypanosome mitochondrial genome and its mechanism of segregation. Moreover, the architecture of the TAC suggests that it may also function in providing a structural and vectorial role during replication of this catenated mass of mitochondrial DNA. We suggest that this complex may represent an extreme form of a more generally occurring mitochondrion/cytoskeleton interaction.
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