ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches.

No abstract is available for this paper.

• Publication year

  1989

• Venue

  Annual Review of Biochemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1146/ANNUREV.BI.58.070189.000551PMID 2528322
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Temperature-sensitive Escherichia coli mutant with an altered initiation codon of the uncG gene for the H+-ATPase gamma subunit

  1988cited by this paper
• Directed mutagenesis of the dicyclohexylcarbodiimide-reactive carboxyl residues in beta-subunit of F1-ATPase of Escherichia coli.

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• Identification of alpha-subunit Lys201 and beta-subunit Lys155 at the ATP-binding sites in Escherichia coli F1-ATPase.

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  1988cited by this paper
• Electroconformational coupling: how membrane-bound ATPase transduces energy from dynamic electric fields.

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• Genes encoding the alpha, gamma, delta, and four F0 subunits of ATP synthase constitute an operon in the cyanobacterium Anabaena sp. strain PCC 7120

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  1988cited by this paper
• Beta subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli, and structural relationship to adenylate kinase.

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• The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly related to F1-ATPase as assessed from the primary structure of its alpha-subunit.

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• Expression of the unc genes in Escherichia coli.

  1988cited by this paper
• Mutagenesis of the alpha subunit of the F1Fo-ATPase from Escherichia coli. Mutations at Glu-196, Pro-190, and Ser-199.

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• A homologous sequence between H+-ATPase (F0F1) and cation-transporting ATPases. Thr-285----Asp replacement in the beta subunit of Escherichia coli F1 changes its catalytic properties.

  1988cited by this paper
• cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases.

  1988cited by this paper
• F0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c.

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• Arginine 328 of the beta-subunit of the mitochondrial ATPase in yeast is essential for protein stability.

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• The γ‐subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence

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• Rate of chase-promoted hydrolysis of ATP in the high affinity catalytic site of beef heart mitochondrial ATPase.

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• The proton pore in the Escherichia coli F0F1-ATPase: substitution of glutamate by glutamine at position 219 of the alpha-subunit prevents F0-mediated proton permeability.

  1988cited by this paper
• Intrinsic membrane sector (Fo) of H+-ATPase (FoF1) from Escherichia coli. Mutations in the alpha subunit give Fo with impaired proton translocation and F1 binding.

  1988cited by this paper
• A mutation in the alpha-subunit of F1-ATPase from Escherichia coli affects the binding of F1 to the membrane.

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• Sequence of the genes for the beta and epsilon subunits of the ATP synthase of Bacillus megaterium QM B1551.

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  1987cited by this paper
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• Biogenesis of mitochondria: a mutation in the 5'-untranslated region of yeast mitochondrial oli1 mRNA leading to impairment in translation of subunit 9 of the mitochondrial ATPase complex.

  1987cited by this paper
• The properties of hybrid F1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs.

  1987cited by this paper
• Evidence for functional heterogeneity among the catalytic sites of the bovine heart mitochondrial F1-ATPase.

  1987cited by this paper
• Loss of unisite and multisite catalyses by Escherichia coli F1 through modification with adenosine tri- or tetraphosphopyridoxal.

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• A gene cluster in the spinach and pea chloroplast genomes encoding one CF1 and three CF0 subunits of the H+-ATP synthase complex and the ribosomal protein S2.

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• CF1ATPase beta- and epsilon-subunit genes are separated in the sweet potato chloroplast genome.

  1987cited by this paper
• ATP synthase from bovine mitochondria. The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs.

  1987cited by this paper
• Directed mutagenesis of the beta-subunit of F1-ATPase from Escherichia coli.

  1987cited by this paper
• Amino acid substitutions in the epsilon-subunit of the F1F0-ATPase of Escherichia coli.

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• The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin of chloroplasts.

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• Characteristics of the formation of enzyme-bound ATP from medium inorganic phosphate by mitochondrial F1 adenosinetriphosphatase in the presence of dimethyl sulfoxide.

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• Dissociation of phosphate from beef heart mitochondrial F1-ATPase. Effect of adenine nucleotides.

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• Epsilon subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis.

  1987cited by this paper
• The pea mitochondrial ATPase subunit 9 gene is located upstream of the ATPase alpha-subunit gene.

  1987cited by this paper
• Genes encoding the beta and epsilon subunits of the proton-translocating ATPase from Anabaena sp. strain PCC 7120

  1987cited by this paper
• Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location.

  1987cited by this paper
• A mutation of the c subunit of the Escherichia coli proton-translocating ATPase that suppresses the effects of a mutant b subunit.

  1987cited by this paper
• Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase Amino acid sequences of β‐subunit tryptic peptides labeled with 2‐azido‐ATP

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• The H+-translocating ATP synthase in Halobacterium halobium differs from F0F1-ATPase/synthase.

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• Escherichia coli F1 ATPase is reversibly inhibited by intra- and intersubunit crosslinking: an approach to assess rotational catalysis.

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  1987cited by this paper
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• The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

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  1987cited by this paper
• A maternal mRNA localized to the animal pole of Xenopus eggs encodes a subunit of mitochondrial ATPase.

  1987cited by this paper
• Coupling factor B is a component of the Fo proton channel of mitochondrial H+-ATPase.

  1987cited by this paper
• P1-(5'-adenosyl)-P2-N-(2-mercaptoethyl)diphosphoramidate. An affinity reagent for demonstrating the presence of Tyr-beta 311 at the hydrolytic site of F1-ATPase.

  1987cited by this paper
• Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.

  1987cited by this paper
• Affinity labeling of adenylate kinase with adenosine diphosphopyridoxal. Presence of Lys21 in the ATP-binding site.

  1987cited by this paper
• 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.

  1987cited by this paper
• The defective proton-ATPase of uncD mutants of Escherichia coli. Identification by DNA sequencing of residues in the beta-subunit which are essential for catalysis or normal assembly.

  1987cited by this paper
• A plasma-membrane associated ATPase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.

  1987cited by this paper
• Mapping of nucleotide-depleted mitochondrial F1-ATPase with 2-azido-[alpha-32P]adenosine diphosphate. Evidence for two nucleotide binding sites in the beta subunit.

  1987cited by this paper
• Different transcript abundance of two divergent ATP synthase subunit 9 genes in the mitochondrial genome of Petunia hybrida

  1987cited by this paper
• Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments from subunit b.

  1987cited by this paper
• In vitro mutated beta subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the alpha and gamma subunits to produce inactive complexes.

  1987cited by this paper
• Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase Photoaffinity labeling and peptide sequencing

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• Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli.

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• Three copies of the beta subunit must be modified to achieve complete inactivation of the bovine mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyladenosine.

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• Conformation-specific antiserum raised against subunit c of ATP synthase (F1F0) from Escherichia coli.

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• Complementation of mutants in the Escherichia coli proton-translocating ATPase by cloned DNA from Bacillus megaterium.

  1986cited by this paper
• Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase.

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• Human F1-ATPase: molecular cloning of cDNA for the beta subunit.

  1986cited by this paper
• Escherichia coli H+-ATPase: loss of the carboxyl terminal region of the gamma subunit causes defective assembly of the F1 portion.

  1986cited by this paper
• Regulation of the mitochondrial ATP synthase/ATPase complex.

  1986cited by this paper
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  1986cited by this paper
• Amino acid substitutions in mitochondrial ATPase subunit 9 of saccharomyces cerevisiae leading to oligomycin or venturicidin resistance

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• A sixth subunit of ATP synthase, an F0 component, is encoded in the pea chloroplast genome

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• Reconstitution of the H+-ATPase complex of Rhodospirillum rubrum by the beta subunit of the chloroplast coupling factor 1.

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