The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel (Q35836734)

10 August 2017

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title

The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel (English)

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10 August 2017

Devenish RJ

1

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10 August 2017

Prescott M

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2

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10 August 2017

Boyle GM

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3

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10 August 2017

Nagley P

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4

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10 August 2017

1 October 2000

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Journal of Bioenergetics and Biomembranes

10 August 2017

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10 August 2017

32

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10 August 2017

507-515

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10 August 2017

5

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https://scigraph.springernature.com/pub.10.1023/a:1005621125812

10 August 2017

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12 December 2020

DNA sequence analysis of the oli1 gene reveals amino acid changes in mitochondrial ATPase subunit 9 from oligomycin-resistant mutants of Saccharomyces cerevisiae.

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Titration of the binding sites for the oligomycin-sensitivity conferring protein in beef heart submitochondrial particles

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Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit

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The assembly of yeast mitochondrial ATP synthase: subunit depletion in vivo suggests ordered assembly of the stalk subunits b, OSCP and d.

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ATP synthase complex from bovine heart mitochondria. Passive H+ conduction through F0 does not require oligomycin sensitivity-conferring protein.

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Heterologous expression, purification, and biochemistry of the oligomycin sensitivity conferring protein (OSCP) from yeast

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Operation of the F(0) motor of the ATP synthase

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Mitochondrial DNA of two independent oligomycin-resistant Chinese hamster ovary cell lines contains a single nucleotide change in the ATPase 6 gene.

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ATP synthase's second stalk comes into focus

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ATP synthase: a tentative structural model

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Single copies of subunits d, oligomycin-sensitivity conferring protein, and b are present in the Saccharomyces cerevisiae mitochondrial ATP synthase

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The ATP synthase of Escherichia coli: structure and function of F(0) subunits

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Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance.

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Oligomycin sensitivity conferring protein (OSCP) of bovine heart mitochondrial ATP synthase: high-affinity OSCP-Fo interactions require a local alpha-helix at the C-terminal end of the subunit

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Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase

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Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine

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ATP synthase from bovine heart mitochondria. In vitro assembly of a stalk complex in the presence of F1-ATPase and in its absence

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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 ofEscherichia coli

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

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Assembly of the mitochondrial membrane system: sequence analysis of a yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci.

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Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents

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Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn

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Amino acid substitutions in mitochondrial ATPase subunit 6 of Saccharomyces cerevisiae leading to oligomycin resistance.

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Topography of the yeast ATP synthase F0 sector

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Oligomycin sensitivity-conferring protein (OSCP) of beef heart mitochondria. Internal sequence homology and structural relationship with other proteins

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A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the delta subunit during ATP hydrolysis

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Assembly of the mitochondrial membrane system. 3. Function and synthesis of the oligomycin sensitivity-conferring protein of yeast mitochondria.

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Catalytic mechanism of F1-ATPase

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Structural interpretations of F(0) rotary function in the Escherichia coli F(1)F(0) ATP synthase

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The ATP synthase--a splendid molecular machine

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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

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ATP synthase from Saccharomyces cerevisiae

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Site-directed cross-linking of b to the alpha, beta, and a subunits of the Escherichia coli ATP synthase

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The functional expression of a rat cDNA encoding OSCP in the yeast Saccharomyces cerevisiae

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Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

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Properties of yeast cells depleted of the OSCP subunit of mitochondrial ATP synthase by regulated expression of the ATP5 gene

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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What makes ATP synthase spin?

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Topography of the yeast ATP synthase F0 sector by using cysteine substitution mutants. Cross-linkings between subunits 4, 6, and f

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12 December 2020

The oligomycin sensitivity conferring protein of rat liver mitochondrial ATP synthase: arginine 94 is important for the binding of OSCP to F1

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Mitochondrial ATP synthase complex. Membrane topography and stoichiometry of the F0 subunits

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Amino acid substitutions in subunit 9 of the mitochondrial ATPase complex of Saccharomyces cerevisiae. Sequence analysis of a series of revertants of an oli1 mit- mutant carrying an amino acid substitution in the hydrophilic loop of subunit 9

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12 December 2020

Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex

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12 December 2020

Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase.

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12 December 2020

Direct observation of the rotation of epsilon subunit in F1-ATPase

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12 December 2020

Stoichiometry of the oligomycin-sensitivity-conferring protein (OSCP) in the mitochondrial F0F1-ATPase determined by an immunoelectrotransfer blot technique

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12 December 2020

Structural interactions of the oligomycin sensitivity-conferring protein in the yeast ATP synthase

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12 December 2020

A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation.

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12 December 2020

Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues

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12 December 2020

Localization of the delta subunit in the Escherichia coli F(1)F(0)-ATPsynthase by immuno electron microscopy: the delta subunit binds on top of the F(1).

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12 December 2020

The F1Fo-ATPase Complex from Bovine Heart Mitochondria: The Molar Ratio of the Subunits in the Stalk Region Linking the F1and FoDomains

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12 December 2020

Monoclonal antibodies against subunits of yeast mitochondrial H+-ATPase

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12 December 2020

Oligomycin sensitivity conferring protein of mitochondrial ATP synthase: deletions in the N-terminal end cause defects in interactions with F1, while deletions in the C-terminal end cause defects in interactions with F0

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12 December 2020

Direct observation of the rotation of F1-ATPase

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12 December 2020

Inhibition of Escherichia coli H+-ATPase by venturicidin, oligomycin and ossamycin

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12 December 2020

Molecular architecture of the rotary motor in ATP synthase

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12 December 2020

The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase

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12 December 2020

Defective energy coupling in delta-subunit mutants of Escherichia coli F1F0-ATP synthase.

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12 December 2020

Amino acid substitutions in mitochondrial ATP synthase subunit 9 of Saccharomyces cerevisiae leading to venturicidin or ossamycin resistance.

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12 December 2020

Entrapment by immobilized metal ion affinity chromatography of assembled yeast mitochondrial ATP synthase containing individual subunits tagged with hexahistidine

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12 December 2020

Eukaryote membrane genetics: the Fo sector of mitochondrial ATP synthase

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12 December 2020

Molecular rotary motors

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12 December 2020

Novel features in the structure of bovine ATP synthase

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12 December 2020

Identification of Amino Acid Substitutions in the Dicyclohexylcarbodiimide-Binding Subunit of the Mitochondrial ATPase Complex from Oligomycin-Resistant Mutants of Saccharomyces cerevisiae

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12 December 2020

The binding change mechanism for ATP synthase--some probabilities and possibilities

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12 December 2020

Sequence analysis of mitochondrial DNA in a mouse cell line resistant to chloramphenicol and oligomycin

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12 December 2020

Molecular models of the structural arrangement of subunits and the mechanism of proton translocation in the membrane domain of F(1)F(0) ATP synthase

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12 December 2020

Identifiers

DOI

10.1023/A:1005621125812

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Dimensions Publication ID

10 August 2017

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