The Mechanism and Regulation of ATP Synthesis by F1-ATPases

Cross, Richard L.

doi:10.1146/annurev.bi.50.070181.003341

Cited by 313 publications

(107 citation statements)

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“…It could also participate in several features of the highly cooperative binding change mechanism of Fr-ATPase [25] as pointed out recently by Fry et al [9]. The binding change mechanism (see [26] for reviews) requires that conformational changes at alternate catalytic sites be tightly coupled to each other. The alternating arrangement of the cy-and &subunits in Fr [27,28] and the results of the uncA @-subunit) mutant studies of Wise et al [29,30] indicate that this involves a pathway of conformational signal transmission from the nucleotide-binding domain of one&subunit through a neighbouring a-subunit to an alternate P-subunit [1,31].…”

Section: Evaluation Of the Model And Its Functional Implicationsmentioning

confidence: 99%

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase

1986

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We propose a working model for the tertiary structure of the nucleotide-binding domain of the @.ubunit of E. coli F,-ATPase, derived from secondary structure prediction and from comparison of the amino acid sequence with the sequences of other nucleotide-binding proteins of known three-dimensional structure. The model is consistent with previously published results of specific chemical modification studies and of analyses of mutations in the b-subunit and its implications for subunit interactions and catalytic mechanism in F,-ATPases are discussed.

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Section: Evaluation Of the Model And Its Functional Implicationsmentioning

confidence: 99%

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase

1986

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“…A zero-time point was obtained by centrifuging the F1 into a solution containing N-ethylmaleimide and EDTA. The reaction was virtually complete at this point (lane 8) and no additional product was formed even with a 30-min incubation period before the addition of EDTA and Nethylmaleimide (lane 12). The majority of the reaction must therefore take place on the column and since Penefsky [I81 found that the most of the applied protein passes though centrifuge columns in the space of 30 s, the reaction must be extremely rapid.…”

Section: Formation and Identification Of Cross-linked Productmentioning

confidence: 98%

“…It is believed that in F1 there are three catalytic sites that act in an alternating manner with strong site-site cooperativity [8]. Much interest is presently directed at the nature of conformational changes which occur within F1 during catalysis.…”

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confidence: 99%

Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

Tozer

Dunn

1986

Eur J Biochem

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Passage of Fl-ATPase through a centrifuge column [Penefsky, H. S. (1979) Methods Enzymol. 56, 527-5301 caused formation of a product with a relative molecular mass of 72000 as determined by sodium dodecyl sulfate/ polyacrylamide gel electrophoresis. The product was identified as cross-linked a and 6 subunits by using Western blots and subunit-specific monoclonal antibodies. The cross-link was reversed by 50 mM dithiothreitol implying that it was a disulfide bridge. Formation of the cross-link was inhibited by 2 mM EDTA and was stimulated in some buffers by the addition of 10 pM CuC12. Time course experiments indicated that the majority of the cross-link formed while the enzyme was passing through the column. Thus the cross-link induced by column centrifugation arose from the rapid, heavy-metal-ion-catalysed oxidation of two sulfhydryl groups, one on the a subunit and one on the 6 subunit, to a disulfide. These results demonstrate that care must be exercised when running proteins through centrifuge columns as potentially deleterious disulfide formation can result.An anti-/3 monoclonal antibody was capable of immunoprecipitating the entire enzyme including the crosslinked subunits, implying that the cross-linked a and 6 subunits were still a part of F1. The formation of the crosslink affected neither the hydrolytic activity of the enzyme nor its susceptibility to inhibition by E subunit. The cross-linked enzyme was unable to bind to F1-depleted membranes in experiments in which soluble F1 and membranes were senarated bv centrifugation. Column centrifugation did not generate the cross-link on membrane- The proton-translocating ATPase of Escherichia coli couples the proton motive force generated by the respiratory chain enzymes to the synthesis of ATP [ l -51. The enzyme consists of two parts: a water-soluble portion named F1 which contains the catalytic activity of the enzyme, and an integral membrane portion named Fo which functions as a protonspecific pore. Fl consists of five types of subunits named a -E in order of decreasing molecular mass and has a subunit stoichiometry of ~3 / 3~y 6~.The catalytic site is thought to reside on the /3 subunits; the a subunits have tight nucleotide binding sites; and the y subunit is thought to organize the a and / 3 subunits into a catalytic active complex. Both the 6 and E subunits are implicated in the binding of the a3p3y complex It is believed that in F1 there are three catalytic sites that act in an alternating manner with strong site-site cooperativity [8]. Much interest is presently directed at the nature of conformational changes which occur within F1 during catalysis. One hypothesis mentioned by Gresser et al. [9] and developed more recently by Cox et al. [lo] that during catalysis there is a rotational movement of the CI -/3 hexamer with respect to the minor subunits. The proximity of each pair of a -p subunits to a particular minor subunit or a particular surface of a minor subunit would be directly reflected in the stage of catalysis the a -pair was undergoing. O...

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“…Latent ATPase activity caused by peptide inhibitors has been demonstrated in mitochondria and chloroplasts (see reviews Cross, 1981 ;Pedersen et al, 1981). Trypsin activated ATPase activity has been demonstrated in membranes of Micrococcus lysodeikticus (Carreira et al, 1976), Mycobacterium phlei (Higashi et al, 1975), Escherichia coli (Nieuwenhuis et al, 1974) and Azotobacter vinelandii (Bhattacharyya & Barnes, 1976).…”

Section: A D G R U N D and J C Ensignmentioning

confidence: 99%

Properties of the Germination Inhibitor of Streptomyces viridochromogenes Spores

Grund¹,

Ensign²

1985

Microbiology

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Germinating spores of Streptonzyces viridochromogenes excreted a substance into the surrounding medium which inhibited germination of another sample of the spores. The germination inhibitor (GI) was produced during submerged culture after exponential growth had ceased. The GI was purified 51-fold following extraction from growth liquor with chloroform. It was soluble in alcohol and water and had a molecular weight of less than 1000. The GI blocked growth and respiration of some Gram-positive bacteria and was an inhibitor of the membrane bound, but not solubilized, calcium-dependent ATPase of germinated spores and mycelia of the producing organism. Several sodium-potassium activated ATPases were also inhibited. All four activities (respiration, growth, germination inhibition, ATPase) co-purified during column and thin-layer chromatography. The GI activities released during germination and produced during growth were identical. A role for the GI antibiotic in regulation of dormancy of spores of the producing organism is discussed.

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The Mechanism and Regulation of ATP Synthesis by F1-ATPases

Cited by 313 publications

References 0 publications

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase

Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

Properties of the Germination Inhibitor of Streptomyces viridochromogenes Spores

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The Mechanism and Regulation of ATP Synthesis by F1-ATPases

Cited by 313 publications

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Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F1‐ATPase

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F1‐ATPase

Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

Properties of the Germination Inhibitor of Streptomyces viridochromogenes Spores

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Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase

Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase