Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.17 (ornithine decarboxylase)
 6,351 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cellular proteins may be designated to fast degradation by their N-terminal amino acids, and especially a N-terminal arginine residue should have an extremely destabilizing effect on cytosol proteins. We investigated the post-translational arginylation of cytosol proteins and especially of ornithine decarboxylase (ODC) by the cytosolic enzyme arginyl transferase by incubation with radioactive L-arginyl-tRNA and isolation of ODC with our monoclonal antibody. Arginylated ODC had a specific radioactivity 8600 times that of the bulk of cytosolic proteins and Edman-degradation of this ODC showed that the post-translational arginylation occurred only at the L-amino-end of the enzyme. The inhibitor of arginyltransferase, L-Glutamyl-L-Valyl-L-Phenylalanine, increased the half-life of ODC in cultured hepatocytes from 39 min to more than 90 min. This post-translational arginylation of ODC and also of other cytosol proteins is reversible. At least 25 different cytosol proteins in addition to ODC can be arginylated in hepatocytes, and at least 15 different proteins can be arginylated in Dictyostelium discoideum. The arginylated proteins are much more rapidly degraded by cellular proteinases, especially by calpains, than those cytosolic proteins which are not arginylated.
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PMID:Post-translational arginylation and intracellular proteolysis. 180 99

We report the physical and genetic mapping of pheV, an Escherichia coli gene for phenylalanine tRNA, to 64 min on the chromosomal map in the near vicinity of speC coding for ornithine decarboxylase.
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PMID:Genetic mapping of pheV, an Escherichia coli gene for tRNA(Phe). 218 6

Ornithine decarboxylase (ODC) was purified 6500-fold from NMRI mouse kidneys under conditions designed to inhibit degradation by proteinases. The enzyme was homogeneous by SDS/polyacrylamide-gel electrophoresis, and the specific activity was among the highest reported. The yield was 70%. A monoclonal antibody against this preparation was generated and used in studies to investigate the half-life of ODC in cultured rat hepatocytes labelled with [35S]methionine. This value was 39 +/- 4 min and was unchanged when either NH4Cl (as a lysosomotropic agent) or leupeptin (as a lysosomal proteinase inhibitor) was added to the culture medium. Thus the intracellular turnover of ODC in cultured hepatocytes occurs mainly in extra-lysosomal compartments. Arginylation of rat ODC was investigated in vitro by incubation with L-[3H]arginyl-tRNA, and the incorporation of the label was compared with that of total cytosolic proteins. Arginylated ODC had a specific radioactivity 8600 times that of the bulk of cytosolic protein. Edman degradation of this ODC showed that the post-translational arginylation occurred only at the alpha-amino end of the enzyme. The inhibitor of arginyl-tRNA:protein arginyltransferase (EC 2.3.2.8), L-glutamyl-L-valyl-L-phenylalanine, increased the half-life of ODC in cultured hepatocytes from 39 min to more than 90 min. The possible significance of the preferential post-translational arginylation of ornithine decarboxylase to its rapid turnover is discussed.
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PMID:Post-translational arginylation of ornithine decarboxylase from rat hepatocytes. 233 97

Rat antizyme gene expression requires programmed, ribosomal frameshifting. A novel autoregulatory mechanism enables modulation of frameshifting according to the cellular concentration of polyamines. Antizyme binds to, and destabilizes, ornithine decarboxylase, a key enzyme in polyamine synthesis. Rapid degradation ensues, thus completing a regulatory circuit. In vitro experiments with a fusion construct using reticulocyte lysates demonstrate polyamine-dependent expression with a frameshift efficiency of 19% at the optimal concentration of spermidine. The frameshift is +1 and occurs at the codon just preceding the terminator of the initiating frame. Both the termination codon of the initiating frame and a pseudoknot downstream in the mRNA have a stimulatory effect. The shift site sequence, UCC-UGA-U, is not similar to other known frameshift sites. The mechanism does not seem to involve re-pairing of peptidyl-tRNA in the new frame but rather reading or occlusion of a fourth base.
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PMID:Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. 781 17

A gram-negative Buttiauxella gaviniae-like organism (LBV449) was isolated from a urine sample of a patient suffering from urine bladder pathology and neurological problems. The isolate was positive for adonitol fermentation and L-arginine dihydrolase and negative for melibiose and L-ornithine decarboxylase. The API 20E code was 3004113. Retrospectively, another isolate (ENT107), from a leg wound, was recovered from our collections and was shown to have similar biochemical characteristics. DNA-DNA hybridization showed 77% similarity between both strains, and strain LBV449 revealed 74% DNA-DNA similarity to the type strain of B. gaviniae. Neither 16S rRNA gene sequencing nor fatty acid analysis were useful for identification. The characteristic tRNA-PCR patterns obtained for these two clinical isolates consisted of fragments with lengths of 102.2, 105.4, 116.6, and 136.9 bp and most resembled the tRNA-PCR pattern obtained for B. gaviniae, but they lacked the B. gaviniae fragments of 88.2 and 239.5 bp. To our knowledge, no clinical cases with Buttiauxella strains have been described thus far.
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PMID:Isolation of Buttiauxella gaviniae from a spinal cord patient with urinary bladder pathology. 1235 4

Paramecium bursaria chlorella virus (PBCV-1) is the prototype of a family of large, icosahedral, plaque-forming, dsDNA viruses that replicate in certain unicellular, eukaryotic chlorella-like green algae. Its 330-kb genome contains approximately 373 protein-encoding genes and 11 tRNA genes. The predicted gene products of approximately 50% of these genes resemble proteins of known function, including many that are unexpected for a virus, e.g., ornithine decarboxylase, hyaluronan synthase, GDP-D-mannose 4,6 dehydratase, and a potassium ion channel protein. In addition to their large genome size, the chlorella viruses have other features that distinguish them from most viruses. These features include: (a) The viruses encode multiple DNA methyltransferases and DNA site-specific endonucleases. (b) The viruses encode at least some, if not all, of the enzymes required to glycosylate their proteins. (c) PBCV-1 has at least three types of introns, a self-splicing intron in a transcription factor-like gene, a spliceosomal processed intron in its DNA polymerase gene, and a small intron in one of its tRNA genes. (d) Many chlorella virus-encoded proteins are either the smallest or among the smallest proteins of their class. (e) Accumulating evidence indicates that the chlorella viruses have a very long evolutionary history.
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PMID:Unusual life style of giant chlorella viruses. 1461 59

We proposed that a group of genes whose expression is enhanced by polyamines at the level of translation in Escherichia coli and mammalian cells be referred to as a "polyamine modulon". In Saccharomyces cerevisiae, proteins whose synthesis is enhanced by polyamines at the level of translation were searched for using a polyamine-requiring mutant of S. cerevisiae deficient in ornithine decarboxylase (YPH499 Deltaspe1). Addition of spermidine to the medium recovered the spermidine content and enhanced cell growth of the YPH499 Deltaspe1 mutant by 3-5-fold. Under these conditions, synthesis of COX4, one of the subunits of cytochrome C oxidase (complex IV), was enhanced by polyamines about 2.5-fold at the level of translation. Accordingly, the COX4 gene is the first member of a polyamine modulon in yeast. Polyamines enhanced COX4 synthesis through stimulation of the ribosome shunting of the stem-loop structures (hairpin structures) during the scanning of the 5'-untranslated region (5'-UTR) of COX4 mRNA by 40S ribosomal subunit-Met-tRNA(i) complex.
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PMID:Polyamine modulon in yeast-Stimulation of COX4 synthesis by spermidine at the level of translation. 1969 41

To adapt to changes in environmental conditions, bacteria regulate their gene expression at the transcriptional but also at the post-transcriptional level, e.g. by small RNAs (sRNAs) which modulate mRNA stability and translation. The conserved RNA chaperone Hfq mediates the interaction of many sRNAs with their target mRNAs, thereby playing a global role in fine-tuning protein production. In this study, we investigated the significance of Hfq for the enteropathogen Yersina enterocolitica serotype O:8. Hfq facilitated optimal growth in complex and minimal media. Our comparative protein analysis of parental and hfq-negative strains suggested that Hfq promotes lipid metabolism and transport, cell redox homeostasis, mRNA translation and ATP synthesis, and negatively affects carbon and nitrogen metabolism, transport of siderophore and peptides and tRNA synthesis. Accordingly, biochemical tests indicated that Hfq represses ornithine decarboxylase activity, indole production and utilization of glucose, mannitol, inositol and 1,2-propanediol. Moreover, Hfq repressed production of the siderophore yersiniabactin and its outer membrane receptor FyuA. In contrast, hfq mutants exhibited reduced urease production. Finally, strains lacking hfq were more susceptible to acidic pH and oxidative stress. Unlike previous reports in other Gram-negative bacteria, Hfq was dispensable for type III secretion encoded by the virulence plasmid. Using a chromosomally encoded FLAG-tagged Hfq, we observed increased production of Hfq-FLAG in late exponential and stationary phases. Overall, Hfq has a profound effect on metabolism, resistance to stress and modulates the production of two virulence factors in Y. enterocolitica, namely urease and yersiniabactin.
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PMID:The RNA chaperone Hfq impacts growth, metabolism and production of virulence factors in Yersinia enterocolitica. 2445 55