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)

The evolution of 5sRNA of 17 organisms ranging from human to bacteria has been studied using a sequence homology analysis. The evolutionary rate of 5sRNA genes has been estimated to be 2.2x10(-10) replacement per one nucleotide site per year. This value is about the same as that of cytochrome C or tRNA's (congruent to 2x10(-10)). A phylogenic tree of these organisms including both eukaryotes and prokaryotes has been constructed from the evolutionary distances (the rate of nucleotide substitution per site) data. The time of divergence of prokaryotes and eukaryotes was estimated to be greater than or congruent to 1.75x10(9) years ago and the branching order in eukaryotic kingdoms is consistent with the traditional order. Blue-green algae separated from the bacterial stem greater than or congruent to 1.3x10(9) years ago after eukaryotes had branched.
J Mol Evol 1975 Dec 31
PMID:Evolution of 5sRNA. 76 86

Closely related proteins show an obvious kinship by having numerous matching amino acids in their aligned sequences. Kinship between anciently separated proteins requires a statistical evaluation to rule out fortuitous similarities. A simple statistic is developed which assumes equal probability for all codon pairs, and a table of critical values for amino acid sequence alignments of lengthnments of length 200 or less is presented. Applying this statistic to V and C regions of immunoglobulin chains, aligned on the basis of shared features of three-dimensional structure, provides evidence that the V and C sequences descended from a common ancestor. Similarly the distant evolutionary relationship of dehydrogenases, flavdoxin, and subtilisin, suggested by structural alignments, is verified. On the other hand, the statistic does not verify a common evolutionary origin for the heme binding pocket in globins and cytochrome bs. Empirical evidence from the distribution of MMD values of amino acid pairs in comparisons of misaligned polypeptide chains and from Monte Carlo trials of sequences aligned with arbitrary gaps supports the validity of the statistic.
J Mol Evol 1977 Apr 29
PMID:Alignment statistic for identifying related protein sequences. 86 19

Spontaneously arising erythromycin-resistant mutants were isolated in the "petite-negative" yeast Kluyveromyces lactis. Two independently arising mutants were studied, in one erythromycin-resistance was conferred by a single dominant nuclear gene, and in the other the resistance was extrachromosomally inherited. In fermentable medium growth of sensitive and resistant strains in presence or absence of erythromycin does not qualitatively change the cytochrome absorption spectra, whereas oxygen uptake of parental strains growing in glucose-medium is affected by the drug. The importance of "petite-negative" yeasts like Kluyveromyces lactis for the study of nucleo-cytoplasmic interrelations is discussed.
Mol Gen Genet 1977 Apr 29
PMID:Chromosomal and extrachromosomal inheritance of erythromycin-resistance in the "petite-negative" yeast Kluyveromyces lactis. 87 30

A fifth cytoplasmic mutation (capr 1) obtained in Podospora anserina is described. In addition to chloramphenicol resistance it confers a strong deficiency in cytochrome aa3 and impairs the germination of ascospores. Genetic analysis shows: 1) strict maternal inheritance of (capr 1) allele; 2) selection against the (capr 1) allele as well in sexual crosses as during vegetative growth; 3) complete reversion of this selection by even low concentration of CAP. On the basis of their cytoplasmic inheritance and altered cytochrome spectra the five cytoplasmic mutations are assumed to be mitochondrial. Analysis of crosses between them allows to class them in 3 loci, 2 of which being closely linked.
Mol Gen Genet 1977 May 20
PMID:Mitochondrial genes in Podospora anserina: recombination and linkage. 88 68

Experimental studies have been undertaken with a view of isolation of the enzyme(s) responsible for the stereospecific oxidation of myo-inositol. A partial fractionation has been achieved and the properties of this extract examined. Results show that the active enzyme may well have a cytochrome component and there is indication that the stereospecificity of Acetomonas oxydans results from permease as opposed to dehydrogenase activity. Kinetic experiments suggest that only one type of active enzyme site is involved in the dehydrogenation of myo-inositol.
Mol Cell Biochem 1977 May 31
PMID:Myo-inositol dehydrogenase(s) from Acetomonas oxydans. 88 81

1. The effect of hexachlorobenzene feeding on liver delta-aminolaevulinate synthase, uroporphyrinogen decarboxylase and cytochrome P 450 was studied at various time-intervals in siderotic and non-siderotic rats. 2 In the non-siderotic group hexachlorobenzene feeding led to a progress decrease in liver uroporphyrinogen decarboxylase activity, accompanied by a progressive increase in delta-aminolaevulinate synthase activity. Cytochrome P 450 concentrations were above normal throughout but fell toward the end of the experiment. 3. Similar but more marked changes were found in the siderotic animals. The fall in uroporphyrinogen decarboxylase activity occurred earlier and was significantly greater in these animals, whereas the increase in delta-aminolaevulinate synthase activity was consistently larger. Liver cytochrome P 450 concentration also rose but to a lesser extent than that in the non-siderotic rats. 4. Hexachlobenzene-induced porphyria would seem to be attributable to inhibition or inactivation of hepatic uroporphyrinogen decarboxylase. Hepatic siderosis has a synergistic effect with hexachlorobenzene on this enzyme and may exert additional effects by promoting cytochrome P 450 turnover.
Clin Sci Mol Med 1977 Aug
PMID:Effects of hexachlorobenzene feeding and iron overload on enzymes of haem biosynthesis and cytochrome P 450 in rat liver. 89 Nov

Two approaches may be used to study the function of cytochrome P-450 in insects: (a) an evaluation of the spectral and catalytic properties of the hemoprotein while associated with microsomal membranes; (b) the solubilization, resolution and purification of the microsomal mixed-function oxidase system. The first approach has provided some understanding of the biochemical factors involved in the metabolism of a variety of compounds, including pesticides, drugs, hormones and many other xenobiotics. However, solubilization of the monooxygenase system allows the study of each of its components individually, providing a better insight on the sequence of events leading to the hydroxylation of a substrate, the type of intermediates formed, and the rate-limiting step(s). This report discusses studies carried out with the monooxygenase system associated with microsomal membranes, as well as procedures to solubilize and partially purify its components from housefly microsomes. The latter involves solubilization with either Triton X-100 or sodium cholate, followed by either ammonium sulfate fractionation, Sephadex G-200, DEAE-Sephadex A-50 column chromatography or by omega-amino-n-octyl-Sepharose 4B affinity chromatography. These procedures have shown that two cytochrome P-450 species (P-450 and P-450I) are present in microsomes isolated from a resistant housefly strain. Induction with either naphthalene or phenobarbital appears to increase cytochrome P-450I preferentially.
Mol Cell Biochem 1976 Jul 30
PMID:Insect cytochrome P-450. 96 61

Rat liver mitochondria were fractionated on the basis of their sedimentation coefficients in the gradient of ficoll. The fractions ("heavy", "middle" and "light" mitochondria) were heterogeneous with regard to the content of protein, DNA, cytochrome a + a3 and respiratory activity. Heterogeneity of mitochondria did not result from the damage or microsomal and lysosomal contamination. The biosynthesis of DNA, RNA and proteins in the different fractions of mitochondria was studied. In vivo incorporation of radioactive precursor into RNA was highest in the fractions of "middle" mitochondria, whereas in vitro the "heavy" mitochondria showed maximum activity in the synthesis of RNA. In vitro DNA synthes was maximum in the fractions of "heavy" mitochondria, protein synthesis in "heavy" and "light" mitochondria. Activity of the synthesis of RNA, DNA and proteins in vitro depends on the content of DNA and cytochrome a + a3 in the different fractions of mitochondria. It is supposed that heterogeneity of mitochondria may be connected with their biogenesis.
Mol Biol (Mosk)
PMID:[Biochemical heterogeneity of mitochondria]. 105 68

1. We have studied the pleiotropic effect of a single-gene mutation of the pts mutant strain 1511 grown at 23 degrees C and 36 degrees C. 2. Growth of the mutant at the non-permissive temperature results in a decrease of respiration rate to about 50% after one generation and to less than 5% after five generations. The cytochrome spectra analysis revealed that only cytochrome c was present after growth at 36 degrees C. 3. Mitochondrial protein synthesis experiments in vivo demonstrated that the protein synthesizing system was not as rapidly inactivated by high temperature as the respiratory system. 4. The recovery of the respiratory capacity of the cells at 23 degrees C is complete but dependent on the de novo synthesis of a temperature sensitive protein.
Mol Gen Genet 1975 Sep 29
PMID:Studies on a temperature sensitive nuclear petite mutant of Saccharomyces cerevisiae: phenotypic reversibility of the mitochondrial functions. 110 55

1. A mutant (ANT 8) of Schizosaccharomyces pombe which shows resistance to antimycin both in vivo and in vitro is characterized biochemically and genetically. 2. In crosses of ANT 8 with auxotrophic strains, resistance to antimycin segregates 2:2 indicating that resistance is conferred by a single nuclear gene. Diploids heterozygous for the resistance gene, however, show segregation of the resistance and sensitivity during mitosis. Possible reasons for this segregation are discussed. 3. Compared with the wild type, the NADH oxidase of ANT 8 requires 13 times as much antimycin for 95% inhibition. After addition of ubiquinone-3, electron transport which is less sensitive to antimycin is found only in the mutant. 4. The resistance of the mutant ANT 8 si due to the much weaker binding of antimycin to mitochondria. As in the wild type, two antimycin binding sites can be separated by binding studies. From the inhibition curves it is evident that binding of antimycin to oxidized mitochondrial particles does not correspond with its inhibitory effect on the partly reduced enzyme in kinetic studies. 5. The peak of the b-cytochrome absorbing at 560.2 nm at 77 degrees K in the wild type is shifted to 561 nm in the mutant. 6. A special preparation method for mutant mitochondrial particles is described, yielding highly active enzymes and CO-insensitive cytochromes. 7. The results are discussed with reference to the components in our model of the respiratory chain, which may be responsible for this type of resistance.
Mol Gen Genet 1975
PMID:Studies on the mechanism of electron trasport in the bc1-segment of the respiratory chain in yeast. III. Isolation and characterization of an antimycin resistant mutant ANT 8 in Schizosaccharomyces pombe. 118 59


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