Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F<sub>1</sub>‐ATPase of <i>Escherichia coli</i>

Ovchinnikov, Yu.A.; Modyanov, Nikolaï N.; Grinkevich, V.A.; Aldanova, N.A.; Trubetskaya, O. E.; Nazimov, Igor V.; Hundal, Torill; Ernster, Lars

doi:10.1016/0014-5793(84)80036-8

Cited by 69 publications

(23 citation statements)

References 9 publications

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“…Comparison of the hydrophobic domain of OSCP with the homologous region in the polypeptide chain of the E. coli &subunit [21-231: shows that the latter is more hydrophilic (60% hydrophobicity, 5 charged residues instead of 2 in OSCP). (More recent analysis shows that a glutamic acid residue is located in position 15 of the OSCP sequence and not glutamine as reported earlier [13].) The hydrophobic domain in the Nterminal sequence of OSCP may explain why this polypeptide remains bound to the membrane sector, while the corresponding subunit in the E. coli ATPase, i.e., the S-subunit, accompanies Fr when the latter is removed from the membrane.…”

Section: Resultssupporting

confidence: 64%

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Ovchinnikov¹,

Modyanov²,

Grinkevich³

et al. 1984

FEBS Letters

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Structural analysis of oligomycin sensitivity~onferring protein (OSCP) revealed repeating sequences (residues l-89, 105-190) suggesting an evolution of the protein by gene duplication. In addition to the reported homology with the d-subunit of Escherichia coli F,ATPase, OSCP also shows a certain homology with the b-subunit of E. coli F,and the ADP/ATP carrier of mitochondria. Uhgomycin sensitivity-conferring protein Subunit Sequence homology Comparative analysisStructural relationship

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Section: Resultssupporting

confidence: 64%

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Ovchinnikov¹,

Modyanov²,

Grinkevich³

et al. 1984

FEBS Letters

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“…These preparations had identical N termini indicating cleavage at the carboxy terminus. The sequence found for the first 13 amino acids was in good accordance with the known sequences of E. coli 6 [34,35] and of beef-heart OSCP, the counterpart of 6 in mitochondria [36], as shown in the following alignment.…”

Section: Resultssupporting

confidence: 55%

Purified subunit δ of chloroplast coupling factor CF₁ reconstitutes photophosphorylation in partially CF₁‐depleted membranes

Engelbrecht

Junge

1988

European Journal of Biochemistry

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The ATP synthase of chloroplasts consists of the proton channel, CFo, and the catalytic part, CF1, which carries nucleotide-binding sites on subunits c1 and 8. The still poorly understood interaction between CFo and the catalytic sites on CF1 is mediated by the smaller subunits y, 6 and E of CF1. We investigated the ability of purified 6 to block proton leakage through CFo channels after their exposure by removal of the CF1 counterpart.Thylakoids were partially depleted of CF1 by EDTA treatment. This increased their proton permeability and thereby reduced the rate of photophosphorylation. Subunit 6 was isolated and purified by FPLC FEBS Lett. 219, 321 -3251. Addition of 6 to EDTA-treated thylakoids reconstituted high rates of phenazine-methosulfate-mediated photophosphorylation. Since 6 does not interact with nucleotides by itself, the reconstitution was due to a reduction of the proton leakage through open CFo channels. The molar ratio of purified 6 over exposed CFo, which started to elicit this effect, was 3 : 1. However, if 6 was added together with purified CF1 lacking 6, in a 1 : 1 molar ratio, the relative amount over exposed CFo was as low as 0.06. This corroborated our previous conclusion [Lill, H., Engelbrecht, S., Schonknecht, G. and Junge, W. (1986) Eur. J . Biochem. 160, 627 -6341 that only a very small fraction of exposed CFo was actually proton-conducting but with a very high unit conductance. CF1 including 6 was apparently rebound preferentially to open CFo channels.Although the ability of 6 to control proton conduction through CFo was evident, it remains to be established whether 6 acts as a gated proton valve or as a conformational transducer in the integral CFoCFl ATPase.The ATP synthase in thylakoid membranes (CFoCFl) couples proton flux to ATP synthesis. It belongs to a class of ATP synthases which also occur in the inner mitochondrial membrane (MFoMFl) and in micro-organisms, e.g. Escherichia coli (EFoEFl) and thermophilic bacteria (TFoTF1). For recent reviews see [l -51. The chloroplast ATP synthase consists of nine different subunits [6, 71. Four of them probably form the membrane-embedded proton channel CFo. Their relative stoichiometry and their quaternary structure are still under debate. The other five subunits form the extrinsic catalytic part, CF1, comprising a (56-58 kda), j (53-56kDa), y (37-39kDa), 6 (19-21 kDa), and E (1 5 kDa). Their stoichiometry is C(&Y61-3~. Electron-microscopic investigations of isolated F1 showed an alternating arrangement of the a and @ subunits in a nearly hexagonal conformation ('cyclohexane chair') [8,9]. A center mass, probably composed of subunits y, 6 and E is slightly shifted out of Correspondence to S. Engelbrecht, Biophysik, Fachbereich Biologie/Chemie, Universitat Osnabriick, BarbarastraDe 1 1, D-4500 Osnabruck, Federal Republic of Germany Abbreviations. CFoCF1, chloroplast ATP synthase; EFoEF1, E. coli ATP synthase; MFoMF1, mitochondrial ATP synthase; CF1, integral chloroplast ATPase; CFo, chloroplast proton channel; CFl(-6), CF1 lacking the 6 ...

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“…The mitochondrial F, subunits are subunit 6, b, OSCP, d , F,, A6L (subunit 8 in yeast) and c (subunit 9 in yeast), with molecular masses of 24.8, 24.7, 21, 18.6, 9, 8 and 7.4 kDa, respectively (Knowles et al, 1971 ;Ovchinnikov et al, 1984;Walker et al, 1987;Fillingame, 1990). The molecular mass of bovine IF, is 9.6 kDa (Frangione et al, 1981).…”

mentioning

confidence: 99%

ATP synthesis in mitochondria

Hatefi

1993

European Journal of Biochemistry

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Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F₁‐ATPase of Escherichia coli

Cited by 69 publications

References 9 publications

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Purified subunit δ of chloroplast coupling factor CF₁ reconstitutes photophosphorylation in partially CF₁‐depleted membranes

ATP synthesis in mitochondria

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Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F1‐ATPase of Escherichia coli

Cited by 69 publications

References 9 publications

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Purified subunit δ of chloroplast coupling factor CF1 reconstitutes photophosphorylation in partially CF1‐depleted membranes

ATP synthesis in mitochondria

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Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F₁‐ATPase of Escherichia coli

Purified subunit δ of chloroplast coupling factor CF₁ reconstitutes photophosphorylation in partially CF₁‐depleted membranes