ArticleProceedings of the National Academy of Sciences of the United States of America2022
Single p197 molecules of the mitochondrial genome segregation system of
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 15 citations in OpenAlex.
- From the flagellum attachment zone to the tripartite attachment complex - widespread cytoskeletal engagement of T. brucei KMP11.Journal of cell science · 2026Article
- Cell cycle ofCurrent zoology · 2026Article
- Disruption of GxxxG motifs in pATOM36 impairs biogenesis of the mitochondrial protein translocase of the outer membrane in Trypanosoma brucei.The Journal of biological chemistry · 2026Article
- 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
- Kozak sequences regulate gene expression in Trypanosoma brucei.Nucleic acids research · 2026Article
- A Practical Guide to Ultrastructural Expansion Microscopy (U-ExM) in Trypanosoma brucei.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A trypanosome-specific complex mediates late-stage processing of cytosolic LSU rRNA.Nucleic acids research · 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
- Molecular characterization of the permanent outer-inner membrane contact site of the mitochondrial genome segregation complex in trypanosomes.PLoS pathogens · 2024Article
- Expansion of metabolically labelled endocytic organelles and cytoskeletal cell structures inMicrobial cell (Graz, Austria) · 2024Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tripartite attachment complex (TAC) couples the segregation of the single unit mitochondrial DNA of trypanosomes with the basal body (BB) of the flagellum. Here, we studied the architecture of the exclusion zone filament (EZF) of the TAC, the only known component of which is p197, that connects the BB with the mitochondrial outer membrane (OM). We show that p197 has three domains that are all essential for mitochondrial DNA inheritance. The C terminus of p197 interacts with the mature and probasal body (pro-BB), whereas its N terminus binds to the peripheral OM protein TAC65. The large central region of p197 has a high α-helical content and likely acts as a flexible spacer. Ultrastructure expansion microscopy (U-ExM) of cell lines exclusively expressing p197 versions of different lengths that contain both N- and C-terminal epitope tags demonstrates that full-length p197 alone can bridge the ∼270-nm distance between the BB and the cytosolic face of the OM. Thus U-ExM allows the localization of distinct domains within the same molecules and suggests that p197 is the TAC subunit most proximal to the BB. In addition, U-ExM revealed that p197 acts as a spacer molecule, as two shorter versions of p197, with the repeat domain either removed or replaced by the central domain of the
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