Philip Stettler

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

The paper identifies TbTim15 as an essential subunit of the trypanosome TIM complex, showing it mediates import of both presequence-containing and mitochondrial carrier proteins.