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Reference: Goyon V, et al. (2008) Yeast Cells Depleted in Atp14p Fail to Assemble Atp6p within the ATP Synthase and Exhibit Altered Mitochondrial Cristae Morphology. J Biol Chem 283(15):9749-58

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Abstract


Within the yeast mitochondrial ATP synthase, subunit h is a small nuclear-encoded protein belonging to the so-called "peripheral stalk" that connects the enzyme catalytic F1 component to the mitochondrial inner membrane. This study examines the role of subunit h in ATP synthase function and assembly using a regulatable, doxycycline-repressible, subunit h gene, to overcome the strong instability of the mitochondrial DNA (mtDNA) previously observed in strains lacking the native subunit h gene. Yeast cells expressing less than 3% of subunit h, but still containing intact mitochondrial genomes, grew poorly on respiratory substrates because of a major impairment of ATP synthesis originating from the ATP synthase, whereas the respiratory chain complexes were not affected. The lack of ATP synthesis in the subunit h depleted (dh) mitochondria was attributed to defects in the assembly/stability of the ATP synthase. A main feature of dh mitochondria was a very low content (< 6%) in the mitochondrially encoded Atp6p subunit, an essential component of the enzyme proton channel, that was in large part due to a slowing down in translation. Interestingly, depletion of subunit h resulted in dramatic changes in mitochondrial cristae morphology, which further supports the existence of a link between the ATP synthase and the folding/biogenesis of the inner mitochondrial membrane.

Reference Type
Journal Article
Authors
Goyon V, Fronzes R, Salin B, di Rago JP, Velours J, Brethes D
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