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Aim24 stabilizes respiratory chain supercomplexes and is required for efficient respiration
Author(s) -
Deckers Markus,
Balleininger Martina,
Vukotic Milena,
Römpler Katharina,
Bareth Bettina,
Juris Lisa,
Dudek Jan
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.006
Subject(s) - respiratory chain , electron transport chain , alternative oxidase , cytochrome c oxidase , biochemistry , mitochondrion , mitochondrial respiratory chain , chemistry , respiration , electron transport complex iv , cytochrome c , yeast , biophysics , coenzyme q – cytochrome c reductase , microbiology and biotechnology , biology , botany
The mitochondrial respiratory chain is essential for the conversion of energy derived from the oxidation of metabolites into the membrane potential, which drives the synthesis of ATP. The electron transporting complexes bc 1 complex and the cytochrome c oxidase assemble into large supercomplexes, allowing efficient energy transduction. Currently, we have only limited information about what determines the structure of the supercomplex. Here, we characterize Aim24 in baker's yeast as a protein, which is integrated in the mitochondrial inner membrane and is required for the structural integrity of the supercomplex. Deletion of AIM24 strongly affects activity of the respiratory chain and induces a growth defect on non‐fermentable medium. Our data indicate that Aim24 has a function in stabilizing the respiratory chain supercomplexes.