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• W1505341782 abstract "Subunit 8 (Y8), a mitochondrially encoded subunit of the F 0 sector of the F 1 F 0 ‐ATP synthase is essential for oxidative phosphorylation. We have previously introduced the technique of allotopic expression to study the structure/function of Y8, whereby an artificial Y8 gene is expressed in the nucleus of cells lacking a functional mitochondrial Y8, thus generating assembly of a functional F 1 F 0 ‐ATPase complex. In this paper we show that when a gene encoding an essentially unmodified version of Y8 is allotopically expressed, ATP synthesis and hydrolysis rates, as well as efficiency of oxidative phosphorylation, were similar to those of the parental wild‐type strain in which Y8 is naturally expressed in mitochondria. We then tested the requirement for the hydrophobicity of the central domain (residues 14–32), which possibly represents a transmembrane stem, by introducing adjacent negative charges at different positions of Y8. One of the variants thus generated, which carries the double substitution Leu23→Asp, Leu24→Asp, when expressed in a strain lacking endogenous Y8, gave rise to cells which grew very slowly by oxidative phosphorylation. Measurement of bioenergetic parameters showed two major defects in these cells relative to control cells allotopically expressing unmodified Y8. First, the activity of the F 1 F 0 ‐ATP synthase was significantly decreased. ATP synthesis and state 3 of respiration were reduced by ≈ 30–40%. ATP hydrolysis was reduced by ≈ 30% and was almost insensitive to the F 0 inhibitor oligomycin. Second, the physical coupling between the two sectors of the enzyme, as well as the stability of the F 1 sector itself, were affected as shown by decreased recovery of F 0 sector [8, 9, b, oligomycin sensitivity‐conferring protein (OSCP), d, h and f] and F 1 sector (α, γ, δ) subunits in immunoprecipitates of ATP synthase. This study indicates that Y8 not only performs an important role in the structure of the mitochondrial complex but also in its activity. We conclude that the hydrophobic character of amino acids 23 and 24 in the middle of the putative transmembrane stem of Y8 is essential for coupling proton transport through F 0 to ATP synthesis on F 1 ." @default.
• W1505341782 created "2016-06-24" @default.
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• W1505341782 date "1999-04-01" @default.
• W1505341782 modified "2023-10-18" @default.
• W1505341782 title "Bioenergetic and structural consequences of allotopic expression of subunit 8 of yeast mitochondrial ATP synthase. The hydrophobic character of residues 23 and 24 is essential for maximal activity and structural stability of the enzyme complex" @default.
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• W1505341782 doi "https://doi.org/10.1046/j.1432-1327.1999.00289.x" @default.
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