The binding of aurovertin to isolated β subunit of F1 (mitochondrial ATPase) stoicheiometry of β subunit in F1

Verschoor, G. J.; Sluis, Peter R. Van Der; Slater, E.C.

doi:10.1016/0005-2728(77)90141-4

Cited by 83 publications

(27 citation statements)

References 21 publications

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“…Thus, when preparations of complex V treated with aurovertin and tributyltin chloride were further treated with oligomycin, the ATP-induced quenching of aurovertin fluorescence was inhibited in the same manner as was shown in Fig. 1 (data not shown) change of aurovertin, which according to available evidence also binds to the p subunits (27,29,30).…”

Section: Resultsmentioning

confidence: 50%

“…In bovine heart and Escherichia coli F1, aurovertin binds to the 83 subunits (27,29,30). In the latter, the binding stoichiometry has been shown to be 1 mol of aurovertin per ,3 subunit (29).…”

Section: Resultsmentioning

confidence: 99%

“…The antibiotic aurovertin is an inhibitor of F1-ATPase (15,16,(24)(25)(26)(27)(28)(29)(30). In bovine heart and Escherichia coli F1, aurovertin binds to the 83 subunits (27,29,30).…”

Section: Resultsmentioning

confidence: 99%

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Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Matsuno‐Yagi¹,

Yagi²,

Hatefi³

1985

Proc. Natl. Acad. Sci. U.S.A.

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Aurovertin is a fluorescent antibiotic that binds to the catalytic beta subunits of the mitochondrial F1-ATPase and inhibits ATP synthesis and hydrolysis. ATP, ADP, and membrane energization in submitochondrial particles (SMP) alter the fluorescence of F1-bound aurovertin. These fluorescence changes are considered to be in response to the conformation changes of F1-ATPase. This paper shows that the ATP-induced fluorescence change of aurovertin bound to SMP or complex V (purified ATP synthase complex F0-F1) is inhibited when these preparations are pretreated with oligomycin or N,N'-dicyclohexylcarbodiimide (DCCD). This inhibition is not seen with isolated F1-ATPase. These and other results have suggested that modifications of the DCCD-binding protein in the membrane sector (F0) of the ATP synthase complex are communicated to F1, thereby altering the binding characteristics of ATP to the beta subunits. By analogy, it is proposed that modifications (e.g., protonation/deprotonation) of the DCCD-binding protein effected by protonic energy alter the conformation of F1 and bring about the substrate/product binding changes that appear to be essential features of the mechanism and regulation of oxidative phosphorylation.

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Section: Resultsmentioning

confidence: 50%

Section: Resultsmentioning

confidence: 99%

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Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Matsuno‐Yagi¹,

Yagi²,

Hatefi³

1985

Proc. Natl. Acad. Sci. U.S.A.

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“…We examined whether 5-FU resistance was affected by addition of exogenous ATP synthase inhibitors. Oligomycin A is an inhibitor of the F 0 part of ATP synthase (39) whereas aurovertin B inhibits the ATP synthase F 1 catalytic sector (40). Interestingly, the combination index values between 5-FU and ATP synthase inhibitors were greater than 1 (data not shown), demonstrating strong antagonism between the two compounds on suppression of cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

Down-regulation of Mitochondrial F1F0-ATP Synthase in Human Colon Cancer Cells with Induced 5-Fluorouracil Resistance

Shin

Yoo²,

Chang³

et al. 2005

Cancer Research

149

140

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5-Fluorouracil (5-FU) is widely used for treatment of advanced colorectal cancer. However, it is common for such patients to develop resistance to 5-FU, and this drug resistance becomes a critical problem for chemotherapy. The mechanisms underlying this resistance are largely unknown. To screen for proteins possibly responsible for 5-FU resistance, cells resistant to 5-FU were derived from human colon cancer cell lines and twodimensional gel electrophoresis-based comparative proteomics was done. Two-dimensional gel electrophoresis data showed there was lower expression of the A subunit of mitochondrial F 1 F 0 -ATP synthase (ATP synthase) in 5-FUresistant cells compared with parent cells. Western blotting showed that expression of other ATP synthase complex subunits was also lower in 5-FU-resistant cell lines and that these resistant cells also showed decreased ATP synthase activity and reduced intracellular ATP content. The ATP synthase inhibitor, oligomycin A, strongly antagonized 5-FUinduced suppression of cell proliferation. When 5-FU sensitivity was compared with ATP synthase activity in six different human colon cancer cell lines, a positive correlation has been found. Furthermore, suppressed ATP synthase d-subunit expression by siRNA transfection increased cell viability in the presence of 5-FU. Bioenergetic dysfunction of mitochondria has been reported as a hallmark of many types of cancers (i.e., down-regulation of ATP synthase B-subunit expression in liver, kidney, colon, squamous oesophageal, and lung carcinomas, as well as in breast and gastric adenocarcinomas). Our findings show that ATP synthase down-regulation may not only be a bioenergetic signature of colorectal carcinomas but may also lead to cellular events responsible for 5-FU resistance. (Cancer Res 2005; 65(8): 3162-70)

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“…The steady state kinetics were measured according to [ 11. The dependence of the enzyme stability on the e-Ns-ATP concentration was measured according to 131. Photoinactivation experiments were carried out by irradiating up to 3 samples simultaneously as given in table 1 with aMineral Light Iamp'UVSL 25 in position 'long wave'.…”

Section: Elsevierlnorth-holland Biomedical Pressmentioning

confidence: 99%

Photoaffinity labelling of a low‐affinity nucleotide binding site on the β‐subunit of yeast mitochondrial F₁‐ATPase

et al. 1979

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The binding of aurovertin to isolated β subunit of F1 (mitochondrial ATPase) stoicheiometry of β subunit in F1

Cited by 83 publications

References 21 publications

Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Down-regulation of Mitochondrial F1F0-ATP Synthase in Human Colon Cancer Cells with Induced 5-Fluorouracil Resistance

Photoaffinity labelling of a low‐affinity nucleotide binding site on the β‐subunit of yeast mitochondrial F₁‐ATPase

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The binding of aurovertin to isolated β subunit of F1 (mitochondrial ATPase) stoicheiometry of β subunit in F1

Cited by 83 publications

References 21 publications

Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.

Down-regulation of Mitochondrial F1F0-ATP Synthase in Human Colon Cancer Cells with Induced 5-Fluorouracil Resistance

Photoaffinity labelling of a low‐affinity nucleotide binding site on the β‐subunit of yeast mitochondrial F1‐ATPase

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Photoaffinity labelling of a low‐affinity nucleotide binding site on the β‐subunit of yeast mitochondrial F₁‐ATPase