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)

Sequence comparisons were made for up to 667 bp of DNA cloned from 14 kinds of Hawaiian Drosophila and five other dipteran species. These sequences include parts of the genes for NADH dehydrogenase (subunits 1, 2, and 5) and rRNA (from the large ribosomal subunit). Because the times of divergence among these species are known approximately, the sequence comparisons give insight into the evolutionary dynamics of this molecule. Transitions account for nearly all of the differences between sequences that have diverged by less than 2%: for these sequences the mean rate of divergence appears to be about 2%/Myr. In comparisons involving greater divergence times and greater sequence divergence, relatively more of the sequence differences are due to transversions. Specifically, the fraction of these differences that are counted as transversions rises from an initial value of less than 0.1 to a plateau value of nearly 0.6. The time required to reach half of the plateau value, about 10 Myr, is similar to that for mammalian mtDNA. The mtDNAs of flies and mammals are also alike in the shape of the curve relating the percentage of positions at which there are differences in protein-coding regions to the time of divergence. For both groups of animals, the curve has a steep initial slope ascribable to fast accumulation of synonymous substitutions and a shallow final slope resulting from the slow accumulation of substitutions causing amino acid replacements. However, the percentage of all sites that can experience a high rate of substitution appears to be only about 8% for fly mtDNA compared to about 20% for mammalian mtDNA.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Evol 1987
PMID:Tempo and mode of sequence evolution in mitochondrial DNA of Hawaiian Drosophila. 312 33

The gene encoding subunit 5 of the NADH dehydrogenase complex (ND 5) has been identified in Oenothera mitochondria from a cDNA clone. The coding region is interrupted by a type II intron of 850 nucleotides and a second intervening sequence of 357 nucleotides. Genomic sequence rearrangement within the first intron creates a nontranscribed partial copy of the gene. The intact ND 5 gene is transcribed in a complex pattern with mRNAs including the 5 S rRNA sequence. Excision of the two introns appears to proceed slowly in vivo since the steady state mitochondrial RNA contains significant proportions of unprocessed precursor molecules.
Mol Gen Genet 1988 Apr
PMID:The NADH-dehydrogenase subunit 5 gene in Oenothera mitochondria contains two introns and is co-transcribed with the 5 S rRNA gene. 316 67

Sheep corpus luteum homogenates were fractionated by centrifugation on continuous sucrose density gradients, with or without digitonin, and gradient fractions were assayed for progesterone, and for a range of intracellular organelle and plasma-membrane markers. Digitonin had little effect on the density distributions of mitochondrial, rough endoplasmic reticulum (RER) and Golgi-endoplasmic reticulum-lysosomal (GERL) membranes. However, digitonin did disrupt lysosomal membranes, leading to release of acid hydrolases, and induced a decrease in buoyant density of NADH-cytochrome c reductase, a putative smooth endoplasmic reticulum (SER) marker. Oxytocin-containing granules were clearly resolved from other organelles accumulating in a sharp peak (density, 1.20 g/cm3). Luteal cell-surface membrane marker activities equilibrated at similar buoyant densities in control gradients, and pretreatment with digitonin induced a marked increase in their buoyant densities. The majority of the progesterone of the sheep corpus luteum equilibrated at a buoyant density of 1.10 g/cm3 in control gradients, and was highly perturbed by digitonin. These fractions also accumulated [3H]progesterone. The buoyant density profile of progesterone in both control and digitonin-treated gradients most closely resembled that of sheep luteal lactogenic receptor, a putative plasma-membrane marker.
Mol Cell Endocrinol 1988 Sep
PMID:Subcellular fractionation of the ovine corpus luteum: association of progesterone with ovine luteal membranes? 319 18

We characterized the genes in the regions of large inverted repeats (IRA and IRB, 10,058 base-pairs each) and a small single copy (SSC 19,813 bp) of chloroplast DNA from Marchantia polymorpha. The inverted repeat (IR) regions contain genes for four ribosomal RNAs (16 S, 23 S, 4.5 S and 5 S rRNAs) and five transfer RNAs (valine tRNA(GAC), isoleucine tRNA(GAU), alanine tRNA(UGC), arginine tRNA(ACG) and asparagine tRNA(GUU)). The gene organization of the IR regions in the liverwort chloroplast genome is conserved, although the IR regions are smaller (10,058 base-pairs) than any reported in higher plant chloroplasts. The small single-copy region (19,813 base-pairs) encoded genes for 17 open reading frames, a leucine tRNA(UAG) and a proline tRNA(GGG)-like sequence. We identified 12 open reading frames by homology of their coding sequences to a 4Fe-4S-type ferredoxin protein, a bacterial nitrogenase reductase component (Fe-protein), five human mitochondrial components of NADH dehydrogenase (ND1, ND4, ND4L, ND5 and ND6), two Escherichia coli ribosomal proteins (S15 and L21), two putative proteins encoded in the kinetoplast maxicircle DNA of Leishmania tarentolae (LtORF 3 and LtORF 4), and a bacterial permease inner membrane component (encoded by malF in E. coli or hisQ in Salmonella typhimurium).
J Mol Biol 1988 Sep 20
PMID:Structure and organization of Marchantia polymorpha chloroplast genome. IV. Inverted repeat and small single copy regions. 319 37

Functional organization of mitochondrial genome (maxicircle kinetoplast DNA (kDNA)) from a flagellate protozoan Crithidia oncopelti was studied by Northern hybridization. A set of overlapping transcripts were mapped in the conserved region of the maxicircle. Several large (3-4 kb) RNAs, overlapping two or more smaller transcripts were found. Four regions produce a couple of RNAs differing in size 50-100 bases. Southern hybridization with several probes from the maxicircle kDNA of Leishmania tarentolae allowed identification of some of the found transcripts as corresponding to NADH dehydrogenase, subunit IV (Nd IV), cytochrome oxidase, subunits I-II (Cox I-II), cytochrome b (Cyt. b), ORF6-genes. Regions, homologous to the probes used are arranged in the same fashion in C. oncopelti kDNA as related genes in L. tarentolae. The divergent region was proved to be poorly transcribed and to produce a set of RNAs from 0.5 to 2.3 kb. Some transcripts of the divergent region seem to hybridize with distant maxicircular fragments. Cross-hybridization of such fragments has shown the absence of the regions of continuous homology.
Mol Biochem Parasitol 1987 Dec
PMID:Transcripts of the maxicircle kinetoplast DNA of Crithidia oncopelti. 343 71

The effect of ethanol consumption by male CF-1 mice on liver microsomal enzyme activities has been investigated. The total microsomal cytochrome P-450 content was increased by 38%, while cytochrome b5 was decreased by 31%, which are characteristic alterations in liver microsomes following ethanol consumption. Other alterations included a decreased NADPH cytochrome c reductase activity and increased NADPH-supported rates of N-nitrosopyrrolidine and aniline hydroxylation. While ethanol consumption did not alter the total metabolism of nicotine, the rates of N- and C-hydroxylation were differently affected. The 5'-hydroxylation of nicotine was increased by 83%, while the N'-oxidation was decreased by 31%. Changes in the microsomal metabolism of the environmental carcinogen 1-nitropyrene included a slight reduction in the overall metabolism, which can be accounted for by a reduction in the formation of one phenolic metabolite, 1-nitropyren-3-ol.
Mol Toxicol
PMID:Differing effects of chronic ethanol consumption by mice on liver microsomal metabolism of xenobiotics: 1-nitropyrene, nicotine, aniline, and N-nitrosopyrrolidine. 344 56

Sequences (ndhA-F) homologous to human mitochondrial genes for components of the respiratory chain NADH dehydrogenase have been found in the chloroplast DNA of tobacco. The ndhA, D, E and F sequences corresponding to the mitochondrial URF1, 4, 4L and 5 are located in the small single copy region, the ndhB sequence corresponding to URF2 in the inverted repeat and the ndhC sequence corresponding to URF3 in the large single copy region of the chloroplast DNA. Northern blot hybridization revealed that all six ndh sequences are actively expressed in the chloroplasts. The ndhA and ndhB sequences contain single introns and the splice sites of their pre-mRNAs were determined by reverse transcription analysis. These findings suggest that potential components of an NADH dehydrogenase are synthesized in the chloroplasts.
Mol Gen Genet 1987 Dec
PMID:Six chloroplast genes (ndhA-F) homologous to human mitochondrial genes encoding components of the respiratory chain NADH dehydrogenase are actively expressed: determination of the splice sites in ndhA and ndhB pre-mRNAs. 348 Oct 22

Plasmodium yoelii nigeriensis infection in albino mice significantly altered the hepatic microsomal mixed function oxidase system. Cytochrome P-450 (the terminal monooxygenase) and other monooxygenases, viz. aniline hydroxylase, aminopyrine-N-demethylase and benzo(a)pyrene hydroxylase were significantly lowered while microsomal heme showed 4-fold increase at 80% parasitaemia. Noticeable impairment in the other components like NADH:cytochrome b5 reductase, NADPH:cytochrome c reductase, cytochrome b5 and glucose-6-phosphatase was also observed. Oral treatment of normal and P. y. nigeriensis infected mice with chloroquine (64 mg per kg body weight for 4 days) caused lowering of mixed function oxidase activities which however showed a recovering trend, a week after cessation of treatment.
Mol Biochem Parasitol 1987 Jul
PMID:Effect of Plasmodium yoelii nigeriensis infection and chloroquine on the hepatic mixed function oxidase system of mice. 362 73

A succinate-coenzyme Q reductase (complex II) was isolated in highly purified form from Ascaris muscle mitochondria by detergent solubilization, ammonium sulfate fractionation and gel filtration on a Sephadex G-200 column. The enzyme preparation catalyzes electron transfer from succinate to coenzyme Q1 with a specific activity of 1.2 mumol coenzyme Q1 reduced per min per mg protein at 25 degrees C. The isolated complex II is essentially free of NADH-ferricyanide reductase, reduced CoQ2-cytochrome c reductase and cytochrome c oxidase and consists of four major polypeptides with apparent molecular weights of 66 000, 27 000, 12 000 and 11 000 and two minor ones with Mr of 36 000 and 16 000. The complex II contained cytochrome b-558, a major constituent cytochrome of Ascaris mitochondria, at a concentration of 3.6 nmol per mg protein, but neither other cytochromes nor quinone. The cytochrome b-558 in the complex II was reduced with succinate. In the presence of Ascaris NADH-cytochrome c reductase (complex I-III) (Takamiya, S., Furushima, R. and Oya, H. (1984) Mol. Biochem. Parasitol. 13, 121-134), the cytochrome b-558 in complex II was also reduced with NADH and reoxidized with fumarate. These results suggest the cytochrome b-558 to function as an electron carrier between NADH dehydrogenase and succinate dehydrogenase in the Ascaris NADH-fumarate reductase system.
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PMID:Electron-transfer complexes of Ascaris suum muscle mitochondria. II. Succinate-coenzyme Q reductase (complex II) associated with substrate-reducible cytochrome b-558. 375 51

Cytochrome P-450 monooxygenase isozymes and NADPH-cytochrome P-450 reductase were detected in the microsomal fraction of rabbit aorta by immunoblotting and by enzymatic activity. The monomeric molecular weights of aortal proteins that cross-reacted with antibodies to cytochrome P-450 forms 2 or 6 and reductase were identical to those of the proteins purified from the liver. The induction of form 6 immunoreactive protein and O-deethylation of 7-ethoxyresorufin (a reaction catalyzed by form 6) was observed in aorta following treatment of rabbits with 2,3,7,8-tetrachlorodibenzo-p-dioxin or beta-naphthoflavone. The amount of reductase protein (equivalent to 22.4 +/- 3.2 activity units/mg of protein) correlated with the cytochrome c reductase activity (18.3 +/- 1.8 units/mg) and was the same for both treated and untreated rabbits. Consistent with immunoblot data, the amount of form 2 was insufficient for detection of activity (N-demethylation of benzphetamine). Significantly, removal of the endothelium, which was confirmed by light microscopy and by scanning electron microscopy, reduced by only 8 to 32% the specific enzymatic activity or content of immunoreactive proteins; only traces of protein or activity were recovered in the endothelial fraction. In studies of the vasculature, the potential of this metabolic pathway for the activation or detoxication of mutagens, carcinogens, toxins, or drugs and metabolism of endogenous substrates warrants consideration, especially in regard to the mutational events reported to be involved in the formation of atherosclerotic plaques.
Mol Pharmacol 1985 Jul
PMID:Cytochrome P-450 monooxygenase system. Localization in smooth muscle of rabbit aorta. 392 49


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