Mitochondrial inner membrane proteins assembly
This study identifies a pathway for oxidation and assembly of mitochondrial inner membrane proteins.
The researchers show that Dbi1 is a conserved mitochondrial inner membrane protein that interacts with the unassembled pool of Tim17, the major component of the presequence translocase.
They also demonstrate that the levels of Dbi1 increase when the levels of unassembled Tim17 increase and Dbi1, through its CxxC motif, is involved in formation of the disulfide bond in Tim17.
In addition, the authors show that Tim22, the central component of the carrier translocase, and Cox20, an assembly chaperone of the Complex IV of the respiratory chain, are substrates of Dbi1.
https://www.embopress.org/doi/full/10.1038/s44319-024-00349-6
