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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Schizosaccharomyces pombe strain EF1 (CBS 356) is haploid, prototrophic, respiratory competent, and of homothallic mating type. From restriction enzyme analysis the length of the mitochondrial genome is 17.3 kilobase pairs, which is in good agreement with the value of 17.1 kilobase pairs determined by electron microscopy. The mitochondrial genome of strain EF1 is thus about 2.3 kilobase pairs shorter than that of strain ade7-50h- (about 19.4 kilobase pairs). A restriction map was constructed for 11 enzymes: For most, but not all of them, the pattern is nearly identical to that of strain ade7-50h-. The genes for the large ribosomal RNA, the subunits 1, 2, and 3 of cytochrome c oxidase, subunits 6 and 9 of ATP synthetase, and cytochrome b were localized by hybridization with mitochondrial DNA probes from Saccharomyces cerevisiae. The gene order was found to be the same in both yeast strains. From Southern hybridization of strain ade7-50h- with nick-translated mitochondrial DNA from strain EF1 it is evident that strain EF1 does not possess the intron, which is present in the cytochrome b gene of Schizosaccharomyces pombe strain ade7-50h-. Crosses between strain ade7-50h- and EF1 demonstrate that both the nuclear and the mitochondrial genomes are able to recombine. The mitochondrial genomes of 2 out of 30 independently isolated hybrids between the two strains are described as the result of recombination between the two parental mitochondrial genomes.
Mol Gen Genet 1984
PMID:The mitochondrial genome of the fission yeast Schizosaccharomyces pombe. 3. Gene mapping in strain EF1 (CBS 356) and analysis of hybrids between the strains EF1 and ade7-50h-. 609 75

The gene for subunit I of cytochrome c oxidase, contained within the OX13 region of yeast mitochondrial DNA, is split and shows a remarkable variation in structure, which is strain-dependent. The most complex form so far characterized is that of the Saccharomyces cerevisiae strain KL14-4A, in which nine or possibly ten exons are separated by eight to nine introns. At least four of these are facultative, two being absent from S. cerevisiae strain D273-10B (sequenced by Bonitz et al., 1980) and a further two lacking from the gene in Saccharomyces carlsbergensis. The complexity of the gene in KL14-4A is also reflected in its transcript pattern. RNA blot hybridization with isolated and cloned DNA fragments of the OX13 region permits visualization of more than 60 RNAs, which show overlapping and discontinuous hybridization behaviour. In the less complex strains D273-10B and S. carlsbergensis, this number is 20 and 11, respectively. These RNAs are most likely intermediates in processing events leading to the appearance of the mature messenger RNA for cytochrome c oxidase subunit I, which we identify as a 2100-nucleotide transcript (18SE). Most of the processing events are dependent on mitochondrial protein synthesis and do not constitute a single obligatory processing pathway. Like other yeast mitochondrial mRNAs, the 18 S RNA contains a long, untranslated 5' flanking sequence (approximately 400 nucleotides). One unusual aspect of splicing events involving OX13 transcripts is the accumulation of three of the excised introns as single-stranded RNA circles. These abundant and stable transcripts appear to be covalently closed. The simplest assumption is that they arise as (by)-products of splicing, but secondary ligation events have not been excluded. Their function is as yet unknown.
J Mol Biol 1983 Feb 15
PMID:Variation, transcription and circular RNAs of the mitochondrial gene for subunit I of cytochrome c oxidase. 618 39

The effects of monoclonal antibodies to bovine and Paracoccus denitrificans cytochromes c (Kuo, L.M. and Davies, H.C. (1983) Mol. Immunol. 20, 827-838) in the reactions of the cytochromes c with cytochrome c oxidase, reductase and peroxidase were studied. Spectrophotometric assays were employed, under conditions where binding of cytochrome c to the enzymes appears to be rate-limiting. Less than stoichiometric amounts of antibodies to P. denitrificans cytochrome c added to the cytochrome rendered some of it nonoxidizable or nonreducible by the P. denitrificans membrane-bound electron transport system and decreased the rate constant with the remaining cytochrome c. The antibodies appear to affect both electron transport reactions (blocking effects) with the oxidase and reductase and binding effects (effects on rate constants) and to distinguish between the two. Different ratios of antibody site to cytochrome c gave different extents of blocking of the reductase as compared with the oxidase reaction. Differences were also apparent in the effect of these antibodies on the reaction of yeast peroxidase and the oxidase with the P. denitrificans cytochrome c. Antibodies to bovine and P. denitrificans cytochromes c had considerably less effect on the reactions of the bovine cytochrome with bovine oxidase and reductase. One antibody was inhibitory to the oxidase reaction with bovine cytochrome c, but not to that with the reductase. Also, an antibody which inhibited the oxidase reaction had no effect on the reaction with yeast peroxidase. The data give evidence that the interaction areas on cytochrome c for oxidase and reductase and peroxidase are not identical, although they may be nearby.
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PMID:Effects of monoclonal antibodies to bovine and Paracoccus denitrificans cytochromes c on reactions with oxidase, reductase and peroxidase. 620 93

Low temperature (77 degrees K) absorption spectra of nonequilibrium states of cytochrome c oxidase produced by reduction of oxidases form protein by thermolysed electrons at 77 degrees K was studied. During reduction of cytochrome oxidase water-glycerol solution by thermolysed electrons at 77 degrees K a nonequilibrium reduced protein is formed. Low temperature (77 degrees K) absorption spectra of the nonequilibrium cytochrome oxidase differs from those reduced by ditionite. It was shown that the oxidation state of cytochrome a3 or addition of cytochrom c have no influence on these spectral changes. It is assumed, that the observed effects are conditioned by structural differences of reduced and oxidased cytochrome oxidase active center. Similar spectral changes were observed for cytochrome oxidase, bound to the mitochondrial membrane. At temperature increasing the low temperature reduced protein is relaxed to a corresponding equilibrium state. The spectral properties of bacterial cytochrome oxidase M. lysodeicticus do not depend on the way of reduction (by dytionite or thermolysed electrons at 77 degrees K).
Mol Biol (Mosk)
PMID:[Absorption spectra and magnetic circular dichroism of heme-containing proteins in nonequilibrium states. VI. Cytochrome c-oxidase]. 624 44

The cytochromes c include subgroups which present a variety of redox functions based on well-defined changes in the basic three-dimensional structure exemplified by the mitochondrial and certain bacterial forms, in particular cytochromes c2. These proteins exhibit overlapping functionality and a graded sequence of structures which provide paradigms well suited for clarification of recognition mechanisms. The character and distribution of cytochromes c will be discussed and approaches to relatedness of structure and function will be described, based on kinetic analyses of cross reactivities of cytochromes c2 with mitochondrial cytochrome c oxidase.
Mol Biol Biochem Biophys 1980
PMID:The cytochromes c: paradigms for chemical recognition. 625 6

Rates of evolution for cytochrome c over the past one billion years were calculated from a maximum parsimony dendrogram which approximates the phylogeny of 87 lineages. Two periods of evolutionary acceleration and deceleration apparently occurred for the cytochrome c molecule. The tempo of evolutionary change indicated by this analysis was compared to the patterns of acceleration and deceleration in the ancestry of several other proteins. The synchrony of these tempos of molecular change supports the notion that rapid genetic evolution accompanied periods of major adaptive radiations. Rates of change at different time in several structural-functional areas of cytochrome c were also investigated in order to test the Darwinian hypothesis that during periods of rapid evolution, functional sites accumulate proportionately more substitutions than areas with no known functions. Rates of change in four proposed functional groupings of sites were therefore compared to rates in areas of unknown function for several different time periods. This analysis revealed a significant increase in the rate of evolution for sites associated with the regions of cytochrome c oxidase and reductase interaction during the period between the emergence of the eutherian ancestor to the emergence of the anthropoid ancestor.
J Mol Evol 1981
PMID:Evolution of cytochrome C investigated by the maximum parsimony method. 626 11

Beef heart cytochrome c oxidase is dimeric in reconstituted membranes and in nonionic detergents at physiological pH [Henderson, R., Capaldi, R. A., & Leigh, J. (1977) J. Mol. Biol. 112, 631; Robinson, N.C., & Capaldi, R. A. (1977) Biochemistry 16, 375], raising the possibility that this aggregation state is a prerequisite for enzymatic activity. A procedure for dissociating the enzyme into monomers is presented. This involves treating the protein with high concentrations of Triton X-100 at pH 8.5. The electron transfer activity of the monomer is comparable to that of the dimer under identical assay conditions. The beef heart cytochrome c oxidase monomer was found to be heterogeneous in hydrodynamic studies, probably due to dissociation of associated polypeptides, including subunit III. Monomer molecular weights in the range 129 000-160 000 were obtained. Previous studies have indicated that shark heart cytochrome c oxidase is monomeric under physiological conditions. Sedimentation equilibrium studies reported here confirm this. The elasmobranch enzyme, with a similar polypeptide composition to that of beef enzyme, was determined to have a molecular weight of 158 000.
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PMID:Electron transfer in monomeric forms of beef and shark heart cytochrome c oxidase. 630 44

Concentric left ventricular hypertrophy was produced in puppies by coarctation banding of the aorta at age 7 weeks. Hemodynamic, morphologic and biochemical studies were carried out 18 months after the operation. Systolic blood pressure proximal to the aortic constriction was 216 +/- 16 mmHg in experimental dogs compared with 115 +/- 5 mmHg in littermate control dogs. Ejection fraction of control and experimental dogs were 59 +/- 4 and 64 +/- 7, respectively. The left ventricular end-diastolic pressure was 6.0 +/- 0.4 in control and 8.4 +/- 1.1 in experimental dogs. There was no sign of overt heart failure in the experimental dogs. Anatomical analysis of different regions of the heart indicated that LV mass in the experimental dogs was increased by about 60%. Ultrastructure of mitochondria in situ, as observed under electron microscope, was normal both in control and hypertrophic hearts. Mitochondria isolated from epicardial and endocardial regions of the stable hypertrophic hearts showed normal rates of respiration, phosphorylation, citrate synthase, and cytochrome c oxidase activities compared to those isolated from hearts of littermate control dogs. It was, therefore, concluded that mitochondrial function is adequately preserved to meet the increased demand for energy in this model of stable cardiac hypertrophy of long duration.
J Mol Cell Cardiol 1983 Apr
PMID:Mitochondrial function in canine experimental cardiac hypertrophy. 630 71

A new mutation has been described which confers resistance to catabolite repression in Saccharomyces cerevisiae. The mutant allele, termed grr-1 for glucose repression-resistant, is characterized by insensitivity to glucose repression for the cytoplasmic enzymes invertase, maltase, and galactokinase, as well as the mitochondrial enzyme cytochrome c oxidase. Hexokinase levels in grr-1 mutants are approximately 3-fold higher than the corresponding activity of the parental strain. Although the grr-1 allele is expressed phenotypically similarly to the hex-1 (hxk-2) and hex-2 mutations described by Entian et al. (1977) and Zimmermann and Scheel (1977) respectively, we have shown genetically and physiologically that grr-1 represents a new class of mutation.
Mol Gen Genet 1984
PMID:Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae. 632 21

Luteal gonadotropin receptors decrease in cows, sheep and rats within 24 h following an injection of a luteolytic dose of prostaglandin (PG) F2 alpha. But it is not known whether this decrease is the specific event, or a reflection of general decline in luteal cell structure, function and metabolism. In order to investigate this possibility, 15 of 21 heifers were given on day 9 of the estrous cycle, a single 500 micrograms injection of Cloprostenol (CO), a synthetic PGF2 alpha analog. These heifers were ovariectomized in groups of 5 at 12, 24 and 36 h after CO. For controls, a group of 6 heifers were ovariectomized just prior to injection of the others. Serum progesterone levels decreased whereas LH levels increased (P less than 0.05) by 12 h with no additional changes observed at 24 or 36 h. The luteal plasma membranes [125I]hCG specific binding, as well as 5'-nucleotidase (5'-NE) activity, decreased by 12 h and continued to decline (P less than 0.05) until 24 h (binding) or 36 h (5'-NE). Scatchard analysis showed that the decrease in [125I]hCG binding was due to a decrease in receptor number rather than a decrease in receptor affinity. The activities of cytochrome c oxidase in mitochondria, NADH cytochrome c reductase in rough endoplasmic reticulum and galactosyl transferase in Golgi decreased while NAD pyrophosphorylase in nuclei virtually disappeared following the injection of CO. The beta-N-acetyl-D-glucosaminidase (a lysosomal hydrolase) activity in the homogenate increased by 12 h and continued to increase up to 36 h.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Endocrinol 1984 Feb
PMID:Decrease of various luteal enzyme activities during prostaglandin F2 alpha-induced luteal regression in bovine. 632 72


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