Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The structure and expression of the pea chloroplast atpH gene, encoding ATP synthase CFo subunit III, have been investigated. The atpH gene is situated between the atpI and atpF genes for CFo subunits IV and I, and encodes a hydrophobic polypeptide of 81 amino acid residues which is very similar to subunit III from other species. Analysis of transcripts from the region of chloroplast DNA encoding ATP synthase subunits IV-III-I-alpha shows a complex pattern of transcription, with large transcripts potentially coding for several subunits and also smaller gene-specific transcripts. Two abundant transcripts of 660 nucleotides (nt) and 980 nt specific for atpH were identified. Primer extension and S1 nuclease protection mapping suggested that the 660-nt transcripts were produced by endonucleolytic processing at the sequence, 5'-UGGAAU.
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PMID:Nucleotide sequence and transcripts of the pea chloroplast gene encoding CFo subunit III of ATP synthase. 212 29

We have isolated the yeast ATP2 gene encoding the beta-subunit of mitochondrial ATP synthase and determined its nucleotide sequence. A fusion between the N-terminal 15 amino acid residues of beta-subunit and the mouse cytosolic protein dihydrofolate reductase (DHFR) was transcribed and translated in vitro and found to be transported into isolated yeast mitochondria. A fusion with the first 35 amino acid residues of beta-subunit attached to DHFR was not only transported but also proteolytically processed by a mitochondrial protease. Amino acid substitutions were introduced into the N-terminal presequence of the beta-subunit by bisulphite mutagenesis of the corresponding DNA. The effects of these mutations on mitochondrial targeting were assessed by transport experiments in vitro using DHFR fusion proteins. All of the mutants, harbourin from one to six amino acid substitutions in the first 14 residues of the presequence, were transported into mitochondria, though at least one of them (I8) was transported and proteolytically processed at a much reduced rate. The I8 mutant beta-subunit also exhibited poor transport and processing in vivo, and expression of this mutant polypeptide failed to complement the glycerol- phenotype of a yeast ATP2 mutant. More remarkably, the expression of I8 beta-subunit induced a more general growth defect in yeast, possibly due to interference with the transport of other, essential, mitochondrial proteins.
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PMID:Transport of the yeast ATP synthase beta-subunit into mitochondria. Effects of amino acid substitutions on targeting. 213 17

The nucleotide sequence of the import precursor of subunit b of rat liver H(+)-ATP synthase has been determined from a recombinant cDNA clone isolated by screening a rat liver cDNA library with a probe DNA. The sequence was composed of 1,124 nucleotides including a coding region for the import precursor of subunit b and noncoding regions of both the 5'- and 3'-sides. The import precursor of subunit b and its mature polypeptide deduced from the open reading frame consisted of 256 and 214 amino acid residues with a molecular weight of 28,867 and 24,628, respectively. The presequence of 42 amino acids could be the import signal peptide which serves to direct the protein into the mitochondrial matrix.
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PMID:cDNA cloning and sequencing for the import precursor of subunit B in H(+)-ATP synthase from rat mitochondria. 214 Sep 36

In vitro transcription and subsequent translation of the cloned Chlamydomonas chloroplast atpB gene was used to study assembly of ATP synthase. Translation in the presence of thylakoids resulted in association of the beta subunit with the membrane. The in vitro synthesized polypeptide bound to the membrane copurified with CF1 on sucrose gradients. This provides more evidence for the self-assembly of CF1.
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PMID:Transcription and translation of the chloroplast atpB-gene and assembly of ATP synthase subunit beta. 214 37

The nucleotide sequence of the import precursor of coupling factor 6 (factor 6) of rat liver H(+)-ATP synthase has been determined from a recombinant cDNA clone isolated by screening a rat liver cDNA library with a probe DNA. The sequence was composed of 458 nucleotides including a coding region for the import precursor of factor 6 and noncoding regions of both the 5'- and 3'-sides. The import precursor of factor 6 and its mature polypeptide deduced from the open reading frame consisted of 108 and 76 amino acid residues with a molecular weight of 12,494 and 8,927, respectively. The presequence of 32 amino acids could be the import signal peptide which serves to direct the protein into the mitochondrial matrix.
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PMID:cDNA cloning and sequencing for the import precursor of coupling factor 6 in H(+)-ATP synthase from rat liver mitochondria. 214 31

The nucleotide sequence of the wheat chloroplast atp I gene encoding CF0 subunit IV of ATP synthase has been determined. The gene encodes a polypeptide of 247 amino acid residues with high sequence similarity to subunit IV from other plant chloroplasts and from cyanobacteria. The polypeptide shows sequence homology to the C-terminus of the F0 alpha subunit of Escherichia coli ATP synthase and subunit 6 of mitochondrial ATP synthase. The atp I gene is co-transcribed with the atp H, atp F and atp A genes for other subunits of ATP synthase in wheat. A gene-fusion of most of the atp I coding region with cro'-lacI'-lacZ' has been constructed in pEX2 and the fusion-protein has been used to raise antibodies in rabbits. The antibodies react with a polypeptide of 17 kDa in wheat thylakoid membranes indicating that the wheat atp I gene is expressed at the protein level. A model for the organisation of the polypeptide in the thylakoid membrane with four membrane-spanning segments is proposed.
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PMID:Expression of the wheat chloroplast gene for CF0 subunit IV of ATP synthase. 215 Mar 49

The incubation of bovine mitochondrial F1-ATPase with 2-hydroxy-5-nitrobenzyl bromide (HNB), a selective reagent toward tryptophan residues in proteins, produced a concentration dependent inactivation of the enzyme and the covalent binding of 0.88 mol reagent/mol F1. Although HNB is highly specific for tryptophan it has also some reactivity toward cysteine, then a pre-treatment of F1 with several sulphydryl reagents has been performed to make the site of reaction clearer. This pre-treatment had neither effects in the binding stoichiometry nor in the extent of catalytic inhibition, suggesting that readly accessible thiol groups are not involved in the reaction with HNB. Since the only tryptophan bearing polypeptide of the bovine mitochondrial F1-ATPase complex is its smallest subunit, subunit-epsilon, this is the most probable candidate for HNB reaction. Therefore it may be inferred that the intactness and/or the correct conformation of this subunit could be important factor(s) for the multisite ATP hydrolytic activity of the enzyme.
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PMID:Does 2-hydroxy-5-nitrobenzyl bromide react with the epsilon-subunit of the mitochondrial F1-ATPase? 215 Apr 81

We have previously shown that the mitochondrial gene atpA, encoding the alpha subunit of F1 ATP synthase, is associated with DNA rearrangements and nuclear-specific transcript patterns in the male-sterile cytoplasm of Ogura radish. Here we present a detailed characterization of this gene from both the normal (fertile) and Ogura (male-sterile) cytoplasms of radish to determine if it is involved in Ogura cytoplasmic male sterility. The normal and Ogura radish atpA loci are virtually identical for 3.8 kb, including a 507 codon open reading frame whose product is approximately 92% identical to other plant ATPA polypeptides. Rearrangement breakpoints have been identified 613 bp 5' and 1663 bp 3' to the atpA coding region. The 5' rearrangement breakpoint is located within a repeated sequence that has been associated with other rearrangement events in radish mitochondria. The previously identified transcript difference results from transcription originating upstream of this rearrangement site. Although the presence of this transcript is affected by nuclear background, analyses in several different sterile and fertile nuclear backgrounds indicate that the presence of this transcript is not strictly correlated with male sterility. In addition, normal levels of ATPA polypeptide are present in sterile plants containing the Ogura cytoplasm.
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PMID:Characterization of radish mitochondrial atpA: influence of nuclear background on transcription of atpA-associated sequences and relationship with male sterility. 215 20

We have characterized the subunit composition of the chloroplast ATP synthase from Chlamydomonas reinhardtii by means of a comparison of the polypeptide deficiencies in a mutant defective in photophosphorylation, with the polypeptide content in purified coupling factor (CF)1 and CF1.CF0 complexes. We could distinguish nine subunits in the enzyme, four of which were CF0 subunits. Further characterization of these subunits was undertaken by immunoblotting experiments, [14C]dicyclohexylcarbodiimide binding and analysis of their site of translation. In particular, we were able to show the presence of an as yet unidentified delta subunit in CF1 from C. reinhardtii. We have identified a 70-kDa peripheral membrane protein in the thylakoid membranes of C. reinhardtii, which is immunologically related to the beta subunit of CF1. We discuss its conceivable ATPase function with respect to the Ca2+-dependent ATPase activity previously reported in the thylakoid membranes from C. reinhardtii.
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PMID:The chloroplast ATP synthase in Chlamydomonas reinhardtii. I. Characterization of its nine constitutive subunits. 252 91

An azide- and vanadate-insensitive, N-ethylmaleimide-sensitive ATPase has been partially purified from a fraction enriched with potassium transporting goblet cell apical membranes of Manduca sexta larval midgut. The properties of the membrane-bound ATPase activity were identical to those of the ATPase activity of highly purified goblet cell apical membranes (Wieczorek, H., Wolfersberger, M. G., Cioffi, M., and Harvey, W. R. (1986) Biochim. Biophys. Acta 857, 271-281). 90% of the azide- and vanadate-insensitive ATPase activity was solubilized by C12E10, leaving 90% of the contaminating azide-sensitive mitochondrial ATPase activity in the pellet after centrifugation at 100,000 x g for 1 h. After discontinuous sucrose gradient centrifugation of the supernatant at 220,000 x g for 1 h nearly all of the azide- and vanadate-insensitive ATPase activity was found in the 30% sucrose fraction without contaminating azide- or vanadate-sensitive ATPase activity. Two prominent bands with relative molecular masses (Mr) of about 600,000 and 900,000, both displaying azide-insensitive and N-ethylmaleimide-sensitive ATPase activity, were found in native microgradient polyacrylamide gel electrophoresis of the 30% sucrose fraction. The two bands could not be separated by anion exchange chromatography. Denaturation of both bands resulted in the same polypeptide pattern (five major bands with Mr 70,000, 57,000, 46,000, 29,000 and 17,000) in sodium dodecylsulfate-polyacrylamide gel electrophoresis, indicating that they represented oligomers of the same protein unit. Substrate and inhibitor specificities of the partially purified ATPase were similar to those of the membrane-bound ATPase activity, whereas salt selectivity differed partly. Altogether, structural and functional properties of the ATPase strongly resemble those of vacuolar-type ATPases.
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PMID:A vacuolar-type ATPase, partially purified from potassium transporting plasma membranes of tobacco hornworm midgut. 252 54


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