Salome Aeschlimann

The paper shows TbTim20 is critical for protein import under low membrane potential in trypanosomes lacking mitochondrial DNA.

The paper identifies four soluble subcomplexes of the outer mitochondrial membrane TAC module in Trypanosoma brucei, suggesting a branched assembly pathway involving a ring-like intermediate.

This paper identifies TAC53 as a novel component of the Tripartite Attachment Complex (TAC) in Trypanosoma brucei, revealing its tubular architecture and role in mitochondrial DNA segregation.

This study identifies the molecular architecture of the TAC60-p166 contact site in Trypanosoma brucei, showing hydrophobic interactions drive its formation rather than electrostatic forces.