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The ATP synthase is involved in generating mitochondrial cristae morphology
Author(s) -
Paumard Patrick,
Vaillier Jacques,
Coulary Bénédicte,
Schaeffer Jacques,
Soubannier Vincent,
Mueller David M.,
Brèthes Daniel,
di Rago JeanPaul,
Velours Jean
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.3.221
Subject(s) - atp synthase , biology , mitochondrion , atp–adp translocase , atp synthase gamma subunit , biogenesis , inner mitochondrial membrane , v atpase , inner membrane , microbiology and biotechnology , biochemistry , translocase of the inner membrane , mitochondrial biogenesis , enzyme , mitochondrial membrane transport protein , atpase , atp hydrolysis , gene
The inner membrane of the mitochondrion folds inwards, forming the cristae. This folding allows a greater amount of membrane to be packed into the mitochondrion. The data in this study demonstrate that subunits e and g of the mitochondrial ATP synthase are involved in generating mitochondrial cristae morphology. These two subunits are non‐essential components of ATP synthase and are required for the dimerization and oligomerization of ATP synthase. Mitochondria of yeast cells deficient in either subunits e or g were found to have numerous digitations and onion‐like structures that correspond to an uncontrolled biogenesis and/or folding of the inner mitochondrial membrane. The present data show that there is a link between dimerization of the mitochondrial ATP synthase and cristae morphology. A model is proposed of the assembly of ATP synthase dimers, taking into account the oligomerization of the yeast enzyme and earlier data on the ultrastructure of mitochondrial cristae, which suggests that the association of ATP synthase dimers is involved in the control of the biogenesis of the inner mitochondrial membrane.