Ornithine Decarboxylase Gene of Neurospora crassa: Isolation, Sequence, and Polyamine-Mediated Regulation of Its mRNA

References

• Akins, R. A., and A. M. Lambowitz. 1985. General method for cloning Neurospora crassa nuclear genes by complementation of mutants. Mol. Cell. Biol. 5:2272–2278.
   PubMedGoogle Scholar
• Arfin, S. M., and R. A. Bradshaw. 1988. Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry 27:7979–7984.
   PubMedGoogle Scholar
• Barnett, G. R., M. Seyfzadeh, and R. H. Davis. 1988. Putrescine and spermidine control degradation and synthesis of ornithine decarboxylase in Neurospora crassa. J. Biol. Chem. 263:10005–10008.
   PubMedGoogle Scholar
• Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513–1523.
   PubMed Web of Science ®Google Scholar
• Brabant, M., L. McConlogue, T. van Daalen Wetters, and P. Coffino. 1988. Mouse ornithine decarboxylase gene: cloning, structure, and expression. Proc. Natl. Acad. Sci. USA 85:2200–2204.
   PubMedGoogle Scholar
• Burnette, W. N. 1981. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacryla- mide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195–203.
   PubMed Web of Science ®Google Scholar
• Cavener, D. R., and S. C. Ray. 1991. Eukaryotic start and stop translation sites. Nucleic Acids Res. 19:3185–3192.
   PubMed Web of Science ®Google Scholar
• Chisholm, D. 1989. A convenient moderate-scale procedure for obtaining DNA from bacteriophage lambda. Biotechniques 7:21–23.
   PubMedGoogle Scholar
• Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloro- form extraction. Anal. Biochem. 162:156–159.
   PubMed Web of Science ®Google Scholar
• Cobianchi, F., and S. H. Wilson. 1987. Enzymes for modifying and labeling DNA and RNA, p. 94–110. In S. H. Berger and A. R. Kimmel (ed.), Guide to molecular cloning techniques. Academic Press, Inc., San Diego, Calif.
   Google Scholar
• Davis, R. H., and F. J. deSerres. 1970. Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17A:79–143.
   Google Scholar
• Davis, R. H., L. V. Hynes, and P. Eversole-Cire. 1987. Nonsense mutations of the ornithine decarboxylase structural gene of Neurospora crassa. Mol. Cell. Biol. 7:1122–1128.
   PubMedGoogle Scholar
• Davis, R. H., G. N. Krasner, J. J. DiGangi, and J. L. Ristow. 1985. Distinct roles of putrescine and spermidine in the regulation of ornithine decarboxylase. Proc. Natl. Acad. Sci. USA 82:4105–4109.
   PubMedGoogle Scholar
• Davis, R. H., M. B. Lawless, and L. A. Port. 1970. Arginaseless Neurospora: genetics, physiology and polyamine synthesis. J. Bacteriol. 102:299–305.
   PubMedGoogle Scholar
• Davis, R. H., and J. L. Ristow. 1989. Uptake, intracellular binding, and excretion of polyamines during growth of Neurospora crassa. Arch. Biochem. Biophys. 271:133–138.
   Google Scholar
• DiGangi, J. J., M. Seyfzadeh, and R. H. Davis. 1987. Ornithine decarboxylase from Neurospora crassa: purification, characterization, and regulation by inactivation. J. Biol. Chem. 262:7889–7893.
   PubMedGoogle Scholar
• Eversole, P., J. J. DiGangi, T. Menees, and R. H. Davis. 1985. Structural gene for ornithine decarboxylase in Neurospora crassa. Mol. Cell. Biol. 5:1301–1306.
   PubMedGoogle Scholar
• Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Feinberg, A. P., and B. Vogelstein. 1984. Addendum to "A technique for radiolabeling restriction endonuclease fragments to high specific activity". Anal. Biochem. 137:266–267.
   PubMed Web of Science ®Google Scholar
• Fonzi, W. A. 1990. Regulation of Saccharomyces cerevisiae ornithine decarboxylase expression in response to polyamines. J. Biol. Chem. 264:18110–18118.
   Google Scholar
• Fonzi, W. A., and P. Sypherd. 1985. Expression of the gene for ornithine decarboxylase of Saccharomyces cerevisiae in Esch-erichia coli. Mol. Cell. Biol. 5:161–166.
   PubMedGoogle Scholar
• Fonzi, W. A., and P. Sypherd. 1987. The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae. J. Biol. Chem. 262:10127–10133.
   PubMed Web of Science ®Google Scholar
• Fu, Y. H., and G. A. Marzluf. 1990. nit-2, the major nitrogen regulatory gene of Neurospora crassa, encodes a protein with a putative zinc finger DNA-binding domain. Mol. Cell. Biol. 10:1056–1065.
   PubMed Web of Science ®Google Scholar
• Fu, Y. H., J. V. Paietta, D. G. Mannix, and G. A. Marzluf. 1989. cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa, encodes a protein with a putative leucine zipper DNA- binding element. Mol. Cell. Biol. 9:1120–1127.
   PubMedGoogle Scholar
• Geever, R. F., L. Huiet, J. A. Baum, B. M. Tyler, V. B. Patel, B. J. Rutledge, M. E. Case, and N. H. Giles. 1989. DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa. J. Mol. Biol. 207:15–34.
   PubMedGoogle Scholar
• Ghoda, L., T. van Daalen Wetters, M. Macrae, D. Ascherman, and P. Coffino. 1989. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science 243:1493–1495.
   PubMedGoogle Scholar
• Ghoda, L., M. A. Phillips, K. E. Bass, C. C. Wang, and P. Coffino. 1990. Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation. J. Biol. Chem. 265:11823–11826.
   PubMed Web of Science ®Google Scholar
• Grens, A., and I. E. Scheffler. 1990. The 5'- and 3'-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency. J. Biol. Chem. 265:11810–11816.
   PubMedGoogle Scholar
• Gupta, M., and P. Coffino. 1985. Mouse ornithine decarboxylase. Complete amino acid sequence deduced from cDNA. J. Biol. Chem. 260:2941–2944.
   Google Scholar
• Gurr, S. J., S. E. Unkles, and J. R. Kinghorn. 1987. The structure and organization of nuclear genes of filamentous fungi, p. 93–139. In J. R. Kinhorn (ed.), Gene structure in eukaryotic microbes. IRL Press, Washington, D.C.
   Google Scholar
• Hayashi, S. (ed.). 1989. Ornithine decarboxylase: biology, enzymology, and molecular genetics. Pergamon Press, Inc., Elmsford, N.Y.
   Google Scholar
• Heby, O., and L. Persson. 1990. Molecular genetics of polyamine synthesis in eukaryotic cells. Trends Biochem. Sci. 15:153–158.
   PubMed Web of Science ®Google Scholar
• Hickok, N. J., P. J. Seppanen, K. K. Kontula, P. A. Janne, C. W. Bardin, and O. A. Janne. 1986. Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3' termini. Proc. Natl. Acad. Sci. USA 83:594–598.
   PubMedGoogle Scholar
• Hölttä, E., and T. Hovi. 1985. Polyamine depletion results in impairment of polyribosome formation and protein synthesis before onset of DNA synthesis in mitogen-activated human lymphocytes. Eur. J. Biochem. 152:229–237.
   PubMedGoogle Scholar
• Ito, K., K. Kashiwagi, S.-I. Watanabe, T. Kameji, S.-I. Hayashi, and K. Igarashi. 1990. Influence of the 5'-untranslated region of ornithine decarboxylase mRNA and spermidine on ornithine decarboxylase synthesis. J. Biol. Chem. 265:13036–13041.
   PubMedGoogle Scholar
• Kameji, T., and A. E. Pegg. 1987. Inhibition of translation of mRNAs for ornithine decarboxylase and S-adenosylmethionine decarboxylase by polyamines. J. Biol. Chem. 262:2427–2430.
   PubMedGoogle Scholar
• Katz, A., and C. Kahana. 1988. Isolation and characterization of the mouse ornithine decarboxylase gene. J. Biol. Chem. 263:7604–7609.
   PubMedGoogle Scholar
• Kiebler, M., R. Pfaller, T. Söllner, G. Griffiths, H. Horstmann, N. Pfanner, and W. Neupert. 1990. Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature (London) 348:610–616.
   PubMedGoogle Scholar
• Kozak, M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229–241.
   PubMed Web of Science ®Google Scholar
• Lowry, O. H., N. J. Rosebrough, A. C. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.
   PubMed Web of Science ®Google Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Manzella, J. M., and P. J. Blackshear. 1990. Regulation of rat ornithine decarboxylase mRNA translation by its 5'-untrans lated region. J. Biol. Chem. 265:11817–11822.
   PubMed Web of Science ®Google Scholar
• Marton, L. J., and D. R. Morris. 1987. Molecular and cellular functions of the polyamines, p. 79–105. In P. P. McCann, A. E. Pegg, and A. Sjoerdsma (ed.), Inhibition of polyamine metabolism. Academic Press, Inc., New York.
   Google Scholar
• Mehdi, H., E. Ono, and K. C. Gupta. 1990. Initiation of translation at CUG, GUG and ACG codons in mammalian cells. Gene 91:173–178.
   PubMedGoogle Scholar
• Metzenberg, R. L., J. N. Stevens, E. U. Selker, and E. Morzyka-Wroblewska. 1984. A method for finding the genetic map position of cloned DNA fragments. Neurospora Newsl. 31:35–39.
   Google Scholar
• Orbach, M. J., E. B. Porro, and C. Yanofsky. 1986. Cloning and characterization of the gene for β-tubulin from a benenomyl- resistant mutant of Neurospora crassa and its use as a dominant selectable marker. Mol. Cell. Biol. 6:2452–2461.
   PubMed Web of Science ®Google Scholar
• Orbach, M. J., M. S. Sachs and C. Yanofsky. 1990. The Neurospora crassa arg-2 locus. Structure and expression of the gene encoding the small subunit of arginine-specific carbamoylphosphate synthetase. J. Biol. Chem. 265:10981–10987.
   PubMed Web of Science ®Google Scholar
• Paluh, J. L., M. J. Orbach, T. L. Legerton, and C. Yanofsky. 1988. The cross-pathway control gene of Neurospora crassa, cpc-1, encodes a protein similar to GCN4 of yeast and the DNA-binding domain of the oncogene v-jun-encoded protein. Proc. Natl. Acad. Sci. USA 85:3728–3732.
   PubMedGoogle Scholar
• Paulus, T. J., C. L. Cramer, and R. H. Davis. 1983. Compartmentation of spermidine in Neurospora crassa. J. Biol. Chem. 258:8608–8612.
   PubMed Web of Science ®Google Scholar
• Paulus, T. J., and R. H. Davis. 1981. Regulation of polyamine synthesis in relation to putrescine and spermidine pools in Neurospora crassa. J. Bacteriol. 145:14–20.
   PubMedGoogle Scholar
• Pegg, A. E. 1986. Recent advances in the biochemistry of polyamines in eucaryotes. Biochem. J. 234:249–262.
   PubMed Web of Science ®Google Scholar
• Persson, L., I. Holm, and O. Heby. 1988. Regulation of ornithine decarboxylase mRNA translation by polyamines. Studies using a cell-free system and a cell line with an amplified ornithine decarboxylase gene. J. Biol. Chem. 263:3528–3533.
   PubMed Web of Science ®Google Scholar
• Pitkin, J., and R. H. Davis. 1990. The genetics of polyamine synthesis in Neurospora crassa. Arch. Biochem. Biophys. 278:386–391.
   PubMedGoogle Scholar
• Pitkin, J., and R. H. Davis. 1991. Unpublished observations..
   Google Scholar
• Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234:364–368.
   PubMed Web of Science ®Google Scholar
• Rosenberg-Hasson, Y., Z. Bercovich, A. Ciechanover, and C. Kahana. 1989. Degradation of ornithine decarboxylase in mammalian cells is ATP-dependent but ubiquitin-independent. Eur. J. Biochem. 185:469–474.
   PubMedGoogle Scholar
• Rosenberg-Hasson, Y., Z. Bercovich, and C. Kahana. 1991. Characterization of sequences involved in mediating degradation of ornithine decarboxylase in cells and in reticulocyte lysate. Eur. J. Biochem. 196:647–651.
   PubMedGoogle Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Sanger, F., S. Niklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Schechtman, M. 1986. A moderate-scale DNA prep for Neurospora. Fungal Genet. Newsl. 33:45–46.
   Google Scholar
• Smith, T. L. 1989. Disparate evolution of yeasts and filamentous fungi indicated by phylogenetic analysis of glyceraldehyde-3- phosphate dehydrogenase trees. Proc. Natl. Acad. Sci. USA 86:7063–7066.
   PubMed Web of Science ®Google Scholar
• Snyder, R. D., and M. L. Edwards. 1991. Effects of polyamine analogs on the extent and fidelity of in vitro polypeptide synthesis. Biochem. Biophys. Res. Commun. 178:1383–1392.
   Google Scholar
• Tabor, C. W., and H. Tabor. 1984. Polyamines. Annu. Rev. Biochem. 53:749–790.
   PubMed Web of Science ®Google Scholar
• Tabor, C. W., and H. Tabor. 1985. Polyamines in microorganisms. Microbiol. Rev. 49:81–99.
   PubMedGoogle Scholar
• Tsunasawa, S., J. W. Stewart and F. Sherman. 1985. Aminoterminal processing of mutant forms of yeast iso-l-cytochrome c. The specificities of methionine aminopeptidase and acetyl-transferase. J. Biol. Chem 260:5382–5391.
   PubMedGoogle Scholar
• van Daalen Wetters, T., M. Macrae, M. Brabant, A. Sittler, and P. Coffino. 1989. Polyamine-mediated regulation of mouse ornithine decarboxylase is posttranslational. Mol. Cell. Biol. 9:5484–5490.
   PubMedGoogle Scholar
• van Steeg, H., C. T. M. van Oostrom, H. M. Hodemaekers, L. Peters, and A. A. M. Thomas. 1991. The translation in vitro of rat ornithine decarboxylase mRNA is blocked by its 5' untranslated region in a polyamine-independent way. Biochem. J. 274:521–526.
   PubMedGoogle Scholar
• Vollmer, S., and C. Yanofsky. 1986. Efficient cloning of genes of Neurospora crassa. Proc. Natl. Acad. Sci. USA 83:4869–4873.
   PubMed Web of Science ®Google Scholar
• Wen, L., J. Huang, and P. J. Blackshear. 1989. Rat ornithine decarboxylase gene. Nucleotide sequence, potential regulatory elements, and comparison to the mouse gene. J. Biol. Chem. 264:9016–9021.
   PubMedGoogle Scholar
• Williams, L. J., and R. H. Davis. 1991. Unpublished observations..
   Google Scholar
• Winqvist, R., T. P. Mäkelä, P. Seppanen, O. A. Janne, L. Alhonen-Hongisto, J. Janne, K. H. Greshik, and K. Alitalo. 1986. Human ornithine decarboxylase sequences map to chromosome regions 2pter p23 and 7cen qter but are not coamplified with the NMYC oncogene. Cytogenet. Cell. Genet. 42:133–140.
   PubMedGoogle Scholar
• Zuker, M., and P. Stiegler. 1981. Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information. Nucleic Acids Res. 9:133–148.
   PubMed Web of Science ®Google Scholar