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The gene for a halophilic glutamate dehydrogenase sequence, transcription analysis and phylogenetic implications

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Summary

We have isolated and sequenced the gene for a putative NADP-dependent glutamate dehydrogenase from the extremely halophilic archaebacterium Halobacterium salinarium. This gene is transcribed as a unique RNA molecule of about 1700 nucleotides. The 5′end of the transcript contains characteristic consensus transcription initiation and promoter sequences observed in halophilic archaebacteria. The encoded polypeptide, with a predicted length of 435 amino acids, shows significant overall homology and conservation of functional domains when compared with different eubacterial and eukaryotic glutamate dehydrogenases. Surprisingly, the archaebacterial protein shares a larger number of identical amino acid residues with homologous polypeptides from higher eukaryotes than with those from unicellular eukaryotes and eubacteria.

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References

  • Austen B, Haberland ME, Smith EL (1980) Secondary structure predictions for the NAD-specific glutamate dehydrogenase of Neurospora crassa. J Biol Chem 225:8001–8004

    Google Scholar 

  • Baldacci G, Guinet F, Tillit J, Zaccai G, De Recondo AM (1990) Functional implications related to the gene structure of the elongation factor EF-Tu from Halobacterium marismortui. Nucleic Acids Res 18:507–511

    Google Scholar 

  • Berghöfer B, Kröckel L, Körtner C, Truss M, Schallenberg J, Klein A (1988) Relatedness of archaebacterial RNA polymerase core subunit to their eubacterial and eukaryotic equivalents. Nucleic Acids Res 16:8113–8128

    Google Scholar 

  • Blanck A, Oesterhelt D (1987) The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J 6:265–273

    Google Scholar 

  • Blumenthal KM, Moon K, Smith EL (1975) Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. J Biol Chem 250:3644–3654

    Google Scholar 

  • Bonete MJ, Camacho ML, Cadenas E (1986) Purification and some properties of NAD+-dependent glutamate dehydrogenase from Halobacterium halobium. Int J Biochem 18:785–789

    Google Scholar 

  • Bonete MJ, Camacho ML, Cadenas E (1987) A new glutamate dehydrogenase from Halobacterium halobium with different coenzyme specificity. Int J Biochem 19:1149–1155

    Google Scholar 

  • Bonete MJ, Camacho ML, Cadenas E (1989) Kinetic mechanism of Halobacterium halobium NAD+-glutamate dehydrogenase. Biochim Biophys Acta 990:150–155

    Google Scholar 

  • Bonete MJ, Camacho ML, Cadenas E (1990) Analysis of the kinetic mechanism of halophilic NADP-dependent glutamate dehydrogenase. Biochim Biophys Acta 1041:305–310

    Google Scholar 

  • Brett M, Chambers GK, Holder AA, Fincham JRS, Wootton JC (1976) Mutational amino acid replacements in Neurospora crassa NADP-specific glutamate dehydrogenase. J Mol Biol 106:122

    Google Scholar 

  • Brown JW, Daniels CJ, Reeve JN (1989) Gene structure, organization, and expression in archaebacteria. Crit Rev Microbiol 16:287–338

    Google Scholar 

  • Chou PY, Fasman GD (1977) β-turns in proteins. J Mol Biol 115:135–175

    Google Scholar 

  • Conover RK, Doolittle WF (1990) Charcterization of a gene involved in histidine biosynthesis in Halobacterium (Haloferax) volcanii: isolation and rapid mapping by transformation of an auxotroph with cosmid DNA. J Bacteriol 172:3244–3249

    Google Scholar 

  • Consalvi V, Chiaraluce R, Politi L, Gambacorta A, De Rosa M, Scandurra R (1991) Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Eur J Biochem 196:459–467

    Google Scholar 

  • Eisenberg H, Wachtel EJ (1987) Structural studies of halophilic proteins, ribosomes, and organelles of bacteria adapted to extreme salt concentrations. Annu Rev Biophys Chem 16:69–92

    Google Scholar 

  • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224:149–155

    Google Scholar 

  • Gallwitz D, Sures I (1980) Structure of a split yeast gene: Complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 77:2546–2550

    Google Scholar 

  • Garnier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120:97–120

    Google Scholar 

  • Gough JA, Murray NE (1983) Sequence diversity among related genes for recognition of specific targets in DNA molecules. J Mol Biol 166:1–19

    Google Scholar 

  • Hawkins AR, Gurr SJ, Montague P, Kinghorn JR (1989) Nucleotide sequence and regulation of expression of the Aspergillus nidulans gdhA gene encoding NADP dependent glutamate dehydrogenase. Mol Gen Genet 218:105–111

    Google Scholar 

  • Johanningmeier U, Bodner U, Wildner FG (1987) A new mutation in the gene coding for the herbicide-binding protein in chlamydomonas. FEBS Lett 211:221–224

    Google Scholar 

  • Julliard JH, Smith EL (1979) Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem 254:3427–3438

    Google Scholar 

  • Kinnaird JH, Fincham RS (1983) The complete nucleotide sequence of the Neurospora crassa am (NADP-specific glutamate dehydrogenase) gene. Gene 26:253–260

    Google Scholar 

  • Lanyi JK (1974) Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev 38:272–290

    Google Scholar 

  • Leicht W, Werber MM, Eisenberg H (1978) Purification and characterization of glutamate dehydrogenase from Halobacterium of the dead sea. Biochemistry 17:4004–4010

    Google Scholar 

  • Mankin AS, Kagramanova VK (1986) Complete nucleotide sequence of the single ribosomal RNA operon of Halobacterium halobium: secondary structure of the archaebacterial 23S rRNA. Mol Gen Genet 202:152–161

    Google Scholar 

  • Mattaj IW, McPherson MJ, Wootton SC (1982) Localisation of a strongly conserved section of coding sequence in glutamate dehydrogenase genes. FEBS Lett 147:21–25

    Google Scholar 

  • McPherson MJ, Wootton JC (1983) Complete nucleotide sequence of the Escherichia coli gdhA gene. Nucleic Acids Res 11: 5257–5266

    Google Scholar 

  • Mevarech M, Leicht W, Werber MM (1976) Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate. Biochemistry 15:2383–2386

    Google Scholar 

  • Moyes WS, Amuro N, Mohana Rao JK, Zalkin H (1985) Nucleotide sequence of yeast gdh1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase. J Biol Chem 260:8502–8508

    Google Scholar 

  • Nagasu T, Hall B (1985) Nucleotide sequence of the GDH gene coding for NADP-specific glutamate dehydrogenase of Saccharomyces cerevisiae. Gene 37:247–253

    Google Scholar 

  • Pearson WR, Lipman DJ (1988) Improved tools for biological sequence comparisons. Proc Natl Acad Sci USA 85:2444–2448

    Google Scholar 

  • Possot O, Sibold L, Aubert J-P (1989) Nucleotide sequence and expression of the glutamine synthetase structural gene, glnA, of the archaebacterium Methanococcus voltae. Res Microbiol 140:355–371

    Google Scholar 

  • Reiter WD, Palm P, Zillig W (1988) Analysis of transcription in the archaebacteirum Sulfolobus indicates that archaebacterial promoters are homologous to eukaryotic pol II promoters. Nucleic Acids Res 16:1–19

    Google Scholar 

  • Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York

    Google Scholar 

  • Sandman K, Krzycki JA, Dobrinski B, Lurz R, Reeve JN (1990) HMf, a DNA-binding protein from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc Natl Acad Sci USA 87:5788–5791

    Google Scholar 

  • Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5467

    Google Scholar 

  • Sioud M, Baldacci G, Forterre P, De Recondo AM (1987) Antitumor drugs inhibit the growth of halophilic archaebacteria. Eur J Biochem 169:231–236

    Google Scholar 

  • Smith EL, Austen BM, Blumenthal KM, Nyc JF (1975) Glutamate dehydrogenases. In: Boyer PD (ed) The enzymes, vol XI. Academic Press, New York, pp 293–367

    Google Scholar 

  • Woese CR, Kandler O, Wheelis ML (1990) Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci USA 87:4576–4579

    Google Scholar 

  • Wootton JC (1974) The coenzyme-binding domains of glutamate dehydrogenases. Nature 252:542–546

    Google Scholar 

  • Yanisch-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103–119

    Google Scholar 

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Authors and Affiliations

  1. Institut de Génétique et Microbiologie, Université Paris-Sud, bât 409, 91405, Orsay cedex, France

    Nadia Benachenhou

  2. Laboratoire de Biologie Moléculaire de la Réplication, UPR 272-CNRS, IRSC 7, rue G. Moquet, 94800, Villejuif, France

    Giuseppe Baldacci

Authors
  1. Nadia Benachenhou
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  2. Giuseppe Baldacci
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Communicated by W. Goebel

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Benachenhou, N., Baldacci, G. The gene for a halophilic glutamate dehydrogenase sequence, transcription analysis and phylogenetic implications. Molec. Gen. Genet. 230, 345–352 (1991). https://doi.org/10.1007/BF00280290

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  • DOI: https://doi.org/10.1007/BF00280290

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