Publications by authors named "Philip Stettler"
Article Synopsis
- - The study focuses on Trypanosoma brucei, a parasitic protozoan, specifically examining the tripartite attachment complex (TAC) that links its mitochondrial genome to the flagellum's basal body.
- - Central to the TAC is the interaction between the outer membrane protein TAC60 and the inner membrane protein p166, which is essential for proper mitochondrial genome segregation during cell division.
- - Researchers used various analytical techniques to identify that the binding between TAC60 and p166 is mainly driven by hydrophobic interactions rather than electrostatic ones, revealing important structural details of this contact site.
Protein import and genome replication are essential processes for mitochondrial biogenesis and propagation. The J-domain proteins Pam16 and Pam18 regulate the presequence translocase of the mitochondrial inner membrane. In the protozoan Trypanosoma brucei, their counterparts are TbPam16 and TbPam18, which are essential for the procyclic form (PCF) of the parasite, though not involved in mitochondrial protein import.
View Article and Find Full Text PDFAll mitochondria import >95% of their proteins from the cytosol. This process is mediated by protein translocases in the mitochondrial membranes, whose subunits are generally highly conserved. Most eukaryotes have two inner membrane protein translocases (TIMs) that are specialized to import either presequence-containing or mitochondrial carrier proteins.
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- - The tripartite attachment complex (TAC) in trypanosomes helps ensure the accurate separation of their single mitochondrial genome during cell division by linking it to the flagella's basal bodies.
- - A model of the TAC’s molecular structure shows how its eight key components connect the flagella’s base with the mitochondrial DNA across membranes.
- - The study also covers how TAC components are imported into mitochondria, assembled, and compares the TAC's function with DNA segregation mechanisms in other organisms, highlighting shared principles.
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.
View Article and Find Full Text PDFThe protist parasite Trypanosoma brucei has a single mitochondrion with a single unit genome termed kinetoplast DNA (kDNA). Faithfull segregation of replicated kDNA is ensured by a complicated structure termed tripartite attachment complex (TAC). The TAC physically links the basal body of the flagellum with the kDNA spanning the two mitochondrial membranes.
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