Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

One mutant of mitochondrial origin resistant to miconazole has been isolated and characterized in S. cerevisiae. The mutation is linked to the locus oli1, the structural gene for subunit 9 of ATPase on mitochondrial DNA. Miconazole inhibited the mitochondrial ATPase of the wild type while the enzyme of the resistant mutant was insensitive to this effect. Levels of ATP decreased to one-third of the control in the wild type in the presence of miconazole, while they were unaffected in the mutant.
Mol Gen Genet 1985
PMID:Mitochondrial resistance to miconazole in Saccharomyces cerevisiae. 316 79

The effect of epidermal growth factor (EGF) on the synthesis of the components of the cholesterol side-chain cleavage enzyme complex (SCC) was studied in rat ovarian granulosa cells. The cells were cultured for 48 h in the presence or absence of EGF (15 ng/ml) and/or FSH (50 ng/ml) after which proteins were radiolabeled by incubation with [35S]methionine followed by immunoprecipitation of newly synthesized P-450scc or adrenodoxin (ISP) with polyclonal antibodies directed against the corresponding proteins from bovine adrenal cortex. In addition the action of EGF on the level of translatable RNA for P-450scc was evaluated using a cell-free translation system programmed with RNA isolated from treated and untreated cells, followed by immunoisolation of newly synthesized proteins. Immunoisolated proteins were separated by polyacrylamide-gel electrophoresis, visualized by fluorography and quantified by densitometry. EGF stimulated progesterone formation by the cells 3-fold and potentiated the FSH-induced stimulation of progesterone formation, but had no effect on cAMP accumulation. EGF also stimulated the synthesis of P-450scc and ISP, and enhanced the FSH-induced synthesis of P-450scc and ISP in a concentration-dependent fashion with a maximal stimulation attained at concentrations ranging from 1.0 to 100 ng/ml. No appreciable changes in the induction pattern were observed when EGF and dibutyryl cyclic AMP (Bt2cAMP) were added together, as compared to when Bt2cAMP was added alone. Neither treatment affected the synthesis of the constitutive mitochondrial enzyme, F1-ATPase. Immunoisolation of P-450scc from the proteins synthesized in a rabbit reticulocyte in vitro translation system programmed with RNA isolated from EGF- and/or FSH-treated cells, revealed that EGF enhanced the FSH-stimulated synthesis of the precursor form of P-450scc.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Endocrinol 1987 Jul
PMID:Effects of epidermal growth factor on the synthesis of the cholesterol side-chain cleavage enzyme complex in rat ovarian granulosa cells in primary culture. 349 31

The partial DNA sequences of two unidentified genes flanking the gene for the large subunit of ribulose bisphosphate carboxylase of Chlamydomonas reinhardii have been reported [(1982) J. Mol. Biol. 162, 775-793]. Based on a comparison of the derived amino acid sequence of one of these genes with the corresponding sequences from Nicotiana tabacum chloroplast DNA and the E. coli atp (unc) operon, one Chlamydomonas gene is identified as coding for the alpha-subunit of the ATP synthase complex.
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PMID:Identification and partial DNA sequence of the gene for the alpha-subunit of the ATP synthase complex of Chlamydomonas reinhardii chloroplasts. 609 53

An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism. The characteristic of the enzyme lies in having a very broad substrate specificity and is inhibited by EDTA and higher concentration of ATP. The enzyme is dependent on bivalent metal ions, Mg++ or Ca++ for its optimum activity. The enzyme is highly sensitive to SH-reagents but insensitive to inhibitors of mitochondrial ATPase or Na+- K+- ATPase. The possible functions of the enzyme in being oriented outside the cell membrane is discussed.
Mol Cell Biochem 1981 Jul 07
PMID:Ecto-ATPase. 611 73

The effect of fluphenazine and related phenothiazine and thioxanthene derivatives on beef heart soluble mitochondrial ATPase (EC 3.6.1.3) was studied under a precise control of the Mg2+-ATP equilibrium. These drugs were shown to be reversible, noncompetitive inhibitors with respect to the substrate (the Mg . ATP complex). The inhibition was found to be dependent on the concentration of free magnesium ions, although free Mg2+ was not essential for the interaction of the inhibitors with the enzymatic protein. Bicarbonate anions, which are known to antagonize the effect of free Mg2+ on the enzyme kinetics, also antagonized the drug-induced inhibition. Concentrations giving 50% inhibition of enzyme activity were in the micromolar range. Inhibitory potencies increased when the pH of the reaction mixture was lowered from 8.2 to 6.9. Cleland [The Enzymes (P. D. Boyer, ed.), Vol. II. Academic Press, New York, 1--65 (1970)] analysis of the inhibition, by means of slope and intercept replots, indicated that the inhibition was the result of the interaction with more than one drug molecule. All drugs tested afforded complete protection against the cold-induced inactivation of soluble mitochondrial ATPase. These results point to a specific mode of inhibition that mimics, in some respects, the action of the natural inhibitor protein of mitochondrial ATPase.
Mol Pharmacol 1982 Mar
PMID:Magnesium-dependent inhibition of beef heart soluble mitochondrial adenosine triphosphatase by tricyclic antipsychotics. 612 79

A newborn female, the second child of consanguineous parents, exhibited general muscle hypotonia, apathy, hepatomegaly and failure to thrive from birth and signs of craniofacial dysmorphia were present. Pipecolic and trihydroxicoprostanoic acid were excreted in the urine and serum transferrin, ferritin and iron were markedly elevated. At the age of 7 weeks the baby died of respiratory insufficiency. Besides malformations of the brain, renal cysts, liver damage with hypoplastic intrahepatic bile ducts and cholestasis, increased storage of iron and cytochemically proven deficiency of peroxisomes in liver and kidney, morphological studied provided evidence of a mitochondrial myopathy in striated muscle with the accumulation of enlarged bizarre mitochondria, showing only minor structural abnormalities. No defects of NADH-reductase, succinate-dehydrogenase or cytochrome-c-oxidase were demonstrated histochemically. Cytochemical-ultrastructural investigation of mitochondrial ATPase revealed activation of the ATP-synthesising enzyme even before the addition of an uncoupler, this indicating loosely coupled oxidative phosphorylation. In addition a high rate of subcellular autophagy with segregation of mitochondria and focal loss of fibrils was present. Muscle damage in Zellweger syndrome appears to be the consequence of complex, interacting metabolic processes. The mitochondrial myopathy thereby induced allows a better understanding of general muscle hypotonia, one of the leading symptoms of this disorder.
Virchows Arch B Cell Pathol Incl Mol Pathol 1984
PMID:Mitochondrial myopathy with loosely coupled oxidative phosphorylation in a case of Zellweger syndrome. A cytochemical-ultrastructural study. 614 41

The isolation and purification of a 600,000 Mr cytosolic Mg2+ -ATPase from human erythrocytes is described. The electrophoretic properties of the native and sodium dodecyl sulphate-dissociated protein are presented and compared with those of the erythrocyte protein cylindrin . The Mg2+-ATPase has a single subunit of Mr 100,000 and it has an isoelectric point of 4.9. From transmission electron microscopy of negatively stained specimens, it is proposed that the Mg2+-ATPase is hexameric, containing two superimposed trimers of the 100,000 Mr subunit, which gives rise to a 13 nm pseudohexagonal particle with a central 3 nm cavity. Varying the orientation of the protein in the negative stain also produces images that are not hexagonal. When orientated on-edge, the protein produces a double-disc image, which is most clearly defined under acidic negative staining conditions with uranyl acetate, when some aggregation of the protein is produced. The ultrastructure of the Mg2+-ATPase is shown to be distinctly different from that of cylindrin . A comparative discussion of the negatively stained transmission electron microscopical images of the Mg2+-ATPase, mitochondrial F1-ATPase and several other oligomeric proteins and enzymes is presented.
J Mol Biol 1984 Apr 25
PMID:Biochemical and ultrastructural characterization of a high molecular weight soluble Mg2+ -ATPase from human erythrocytes. 614 98

The nucleotide sequence has been determined of a 12,368 base-pair region of DNA cloned from the non-sulphur photosynthetic bacterium Rhodopseudomonas blastica. It contains a cluster of six genes of which five encode the subunits of F1-ATPase; the sixth codes for an unknown protein. The genes are arranged in the same order as in the Escherichia coli unc operon, except that the unknown gene is placed between those for gamma and beta subunits. Neither the genes for F0 subunits, nor a homologue of the E. coli uncI gene is associated with this locus. The six genes are transcribed from a single promoter and we have designated this region the R. blastica atp operon. The two distal genes, beta and epsilon, may also be transcribed from a second promoter. Initiation and termination points for transcription have been identified by primer extensions and S1 nuclease mapping experiments. Signals involved in initiation of translation (Shine and Dalgarno sequences) and termination of transcription in the photosynthetic bacterium resemble those in E. coli. However, no common features can be identified in these two bacteria between 5' regions adjacent to sites of initiation of transcription. The sequence also contains a gene that encodes a protein homologous to discoidin, a cell surface lectin of Dictyostelium discoideum thought to be involved in cell--cell aggregation. Seven other reading frames have not been identified.
J Mol Biol 1984 Oct 25
PMID:Rhodopseudomonas blastica atp operon. Nucleotide sequence and transcription. 620 4

The reaction of Trypanosoma cruzi Mg2+-stimulated adenosine triphosphatase (ATPase, coupling factor 1, or F1) with phenylglyoxal, a dicarbonylic compound, resulted in a rapid loss of its enzymatic activity. The inactivation showed pseudo-first-order kinetics with both membrane-bound and soluble F1-ATPase, the rate of the enzyme inactivation being faster in bicarbonate buffer (pH 7.9) than in borate buffer (pH 8.0). The log (pseudo-first-order rate constant) vs. log(phenylglyoxal concentration) plots obtained with the membrane-bound and soluble F1-ATPase in bicarbonate buffer, and also with F1 in borate buffer, had slopes of near 1.0 while the plot for the membrane-bound ATPase in borate buffer had a slope of 1.6. Second-order rate constants (in mM-1 X min-1) were 55 (for both ATPase preparations in bicarbonate buffer) and 34 (for the membrane-bound ATPase in borate buffer). When the reaction was performed in the presence of ATP, the rate of inactivation was significantly decreased. It is concluded that, as in the mammalian F1-ATPase, arginyl residues play an essential role in T. cruzi mitochondrial ATPase, probably at the hydrolytic site.
Mol Biochem Parasitol 1982 Jun
PMID:Phenylglyoxal inactivation of the mitochondrial adenosine triphosphatase from Trypanosoma cruzi. 621 57

The combined use of proteolytic digestion and lactoperoxidase catalyzed labelling with [125I] applied to membrane-bound or soluble pure F1-ATPase from Micrococcus lysodeikticus has allowed us to establish the topography of its alpha, beta, gamma and delta subunits within the protein molecule and with respect to the plane of the membrane. The beta subunit is most externally located to the membrane bilayer looking towards the cytoplasmic face, a position consistent with its proposed catalytic role. The alpha and gamma subunits lie in an intermediate layer between the beta subunits and the membrane, in which the gamma subunit occupies a central position within the F1-ATPase molecule in contact with the alpha subunit. The delta subunit appears to be tightly bound to the F0 component of the ATPase complex, probably buried in the membrane bilayer. A molecular arrangement of M. lysodeikticus ATPase is proposed that, taking into account the subunit stoichiometry alpha 3 beta 3 gamma 2 delta 2 (MW 420 000), accommodates the role assigned to each subunit and most, if not all, the known properties of this bacterial energy-transducing protein.
Mol Cell Biochem 1983
PMID:Topography of the subunits of Micrococcus lysodeikticus F1-ATPase. 622 69


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