ATP synthase from bovine mitochondria

Walker, John E.; Runswick, Michael J.; Poulter, Linda

doi:10.1016/0022-2836(87)90611-5

Cited by 138 publications

(44 citation statements)

References 63 publications

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“…In vitro assembly experiments described below have helped to confirm that subunits b and d are also stalk components. The hydrophobic profile of subunit b [28] has two consecutive hydrophobic stretches from amino acids 3&53 and 58-79 that could form the arms of an a-helical hair-pin spanning the inner membrane twice. The remainder of its sequence is highly charged and is capable of making important interactions either with other subunits in the stalk or, as in the analogous subunit b in the bacterial F,F,-ATPases, with F, subunits.…”

Section: F1 -Atpasementioning

confidence: 99%

“…Homologues of bovine b are present in the rat [29] and yeast [30] mitochondrial enzymes, and a human homologue has also been sequenced [31]. Subunit d has no extensive hydrophobic regions in its sequence [28], and, like F,, it is probably attached to the matrix surface of the inner mitochondrial membrane. Homologues of bovine d have been identified in the yeast and rat enzymes [32,33].…”

Section: F1 -Atpasementioning

confidence: 99%

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The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

Walker

Collinson

1994

FEBS Letters

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The extrinsic and intrinsic membrane sectors of F,F,-ATPases are linked by a slender stalk 4&50 A in length. The stalk transmits the energy produced by oxidative or photosynthetic phosphorylation from the intrinsic sector, FO, to the catalytic sites in the extrinsic F, sector. How this is achieved is unknown, but long-range conformational changes linked to transmembrane proton transport may be involved. In bacterial and chloroplast F,F,-ATPases, the stalk is probably a composite of subunits 6 and E, part of the y-subunit, and the extrinsic membrane domains of 2 subunits (identical or non-identical according to the species) that are bound to the membrane by their N-terminal regions. The stalk in the bovine mitochondrial enzyme appears to be more complex, and the y, 6, E, OSCP, Fe, b and d subunits all contribute to it. A bovine stalk complex has been assembled in vitro from bacterially expressed OSCP, F,, b and d, both in the presence and in the absence of F,-ATPase. One molecule of each of these subunits is present in the assembled complexes, as there is also in each native F,F,-ATPase assembly. Providing that suitable crystals can be obtained, the stalk complex and the F, stalk complex may permit the high resolution structure of bovine F,-ATPase to be extended into the stalk domain.

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Section: F1 -Atpasementioning

confidence: 99%

Section: F1 -Atpasementioning

confidence: 99%

The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

Walker

Collinson

1994

FEBS Letters

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“…Altendorf, unpublished results). This is possibly due to the fact that Cys2l is located in the hydrophobic N-terminal region, whereas Cys197 of mitochondrial subunit h is located in the hydrophilic part of the polypeptide chain, close to the C-terminus [54]. In addition, incubation of submitochondrial particles partially depleted of F, with diamide, which reacts with vicinal thiol groups, caused a threefold stimulation of proton translocation, possibly due to crosslinking between subunit h of mitochondrial F, and subunit 1) of FI [51, 531. …”

Section: Discussionmentioning

confidence: 99%

Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Escherichia coli

Kauffer

Deckers-Hebestreit

Altendorf

1991

European Journal of Biochemistry

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The Fo complex of the ATP synthase (F1Fo) of Escherichia coli contains only two cysteinly residues, Cys21, of the two copies of subunit b. Modification of Cys21 with the hydrophobic maleimide N‐(7‐dimethylamino‐4‐methyl‐coumarinyl)maleimide resulted in impairment of Fo functions [Schneider, E. & Altendorf, K. (1985) Eur. J. Biochem. 153, 105–109]. We replaced this resdue (via cassette mutagenesis) by Ser, Gly, Ala, Thr, Asp and Pro. None of the replacements resulted in detectable alterations of the function of the ATP synthase, making a functional role for these sulfhydryl residues unlikely. Due to its high tolerance towards amino acid substitutions, the region around Cys21 seems not to be a protein‐protein contact area.

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“…Our studies show that the PVP (FoI) protein of the mitochondrial enzyme plays a critical role in proton conduction by Fo. Previous results from our laboratories showed that this subunit, encoded by a nuclear gene, and consisting of 214 residues [38], extends out of the M side of the membrane where it is covered by Fl [15].…”

Section: Reconstitution Studiesmentioning

confidence: 99%

Mitochondrial F₀F₁ H⁺‐ATP synthase Characterization of F₀ components involved in H⁺ translocation

et al. 1989

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The membrane F0 sector of mitochondrial ATP synthase complex was rapidly isolated by direct extraction with CHAPS from F,-depleted submitochondrial particles. The preparation thus obtained is stable and can be reconstituted in artificial phospholipid membranes to result in oligomycin-sensitive proton conduction, or recombined with purified F, to give the oligomycin-sensitive F,F,-ATPase complex. The F0 preparation and constituent polypeptides were characterized by SDSpolyacrylamide gel electrophoresis and immunoblot analysis. The functional role of F,, polypeptides was examined by means of trypsin digestion and reconstitution studies. It is shown that, in addition to the 8 kDa DCCD-binding protein, the nuclear encoded protein ) J. Mol. Biol. 197, 89-1001

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ATP synthase from bovine mitochondria

Cited by 138 publications

References 63 publications

The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Escherichia coli

Mitochondrial F₀F₁ H⁺‐ATP synthase Characterization of F₀ components involved in H⁺ translocation

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ATP synthase from bovine mitochondria

Cited by 138 publications

References 63 publications

The role of the stalk in the coupling mechanism of F1F0‐ATPases

The role of the stalk in the coupling mechanism of F1F0‐ATPases

Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Escherichia coli

Mitochondrial F0F1 H+‐ATP synthase Characterization of F0 components involved in H+ translocation

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The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

The role of the stalk in the coupling mechanism of F₁F₀‐ATPases

Mitochondrial F₀F₁ H⁺‐ATP synthase Characterization of F₀ components involved in H⁺ translocation