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J Bacteriol. Feb 1992; 174(3): 899–907.
PMCID: PMC206168

Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus.

Abstract

The N-terminal amino acid sequence of purified acetaldehyde dehydrogenase II (AcDH-II) from ethanol-grown cells of Alcaligenes eutrophus was determined. By using oligonucleotides deduced from this sequence the structural gene for AcDH-II, which was referred to as acoD, was localized on a 7.2-kbp EcoRI restriction fragment (fragment D), which has been cloned recently (C. Fründ, H. Priefert, A. Steinbüchel, and H. G. Schlegel, J. Bacteriol. 171:6539-6548, 1989). A 2.8-kbp PstI subfragment of D, which harbored acoD, was sequenced. It revealed an open reading frame of 1,518 bp, encoding a protein with a relative molecular weight of 54,819. The insertions of Tn5::mob of two transposon-induced mutants of A. eutrophus, which were impaired in the catabolism of acetoin, were mapped 483 or 1,359 bp downstream from the translational start codon of acoD. The structural gene was preceded by a putative Shine-Dalgarno sequence. The transcriptional start site 57 bp upstream of acoD was identified and was preceded by a sequence which exhibited a striking homology to the enterobacterial sigma 54-dependent promoter consensus sequence. This was in accordance with the observation that the expression of acoD and of other acetoin-catabolic genes depended on the presence of an intact rpoN-like gene. Alignments of the amino acid sequence deduced from acoD with the primary structures of aldehyde dehydrogenases from other sources revealed high degrees of homology, amounting to 46.5% identical amino acids.

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  • Abriola DP, Fields R, Stein S, MacKerell AD, Jr, Pietruszko R. Active site of human liver aldehyde dehydrogenase. Biochemistry. 1987 Sep 8;26(18):5679–5684. [PubMed]
  • Bibb MJ, Findlay PR, Johnson MW. The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene. 1984 Oct;30(1-3):157–166. [PubMed]
  • Buck M, Woodcock J, Cannon W, Mitchenall L, Drummond M. Positional requirements for the function of nif-specific upstream activator sequences. Mol Gen Genet. 1987 Nov;210(1):140–144. [PubMed]
  • Devereux J, Haeberli P, Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. [PMC free article] [PubMed]
  • Dunn TJ, Koleske AJ, Lindahl R, Pitot HC. Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats. J Biol Chem. 1989 Aug 5;264(22):13057–13065. [PubMed]
  • Eberz G, Friedrich B. Three trans-acting regulatory functions control hydrogenase synthesis in Alcaligenes eutrophus. J Bacteriol. 1991 Mar;173(6):1845–1854. [PMC free article] [PubMed]
  • Farrés J, Guan KL, Weiner H. Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences. Eur J Biochem. 1989 Mar 1;180(1):67–74. [PubMed]
  • Friedrich B, Hogrefe C, Schlegel HG. Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcaligenes eutrophus. J Bacteriol. 1981 Jul;147(1):198–205. [PMC free article] [PubMed]
  • Fründ C, Priefert H, Steinbüchel A, Schlegel HG. Biochemical and genetic analyses of acetoin catabolism in Alcaligenes eutrophus. J Bacteriol. 1989 Dec;171(12):6539–6548. [PMC free article] [PubMed]
  • Fukaya M, Tayama K, Tamaki T, Tagami H, Okumura H, Kawamura Y, Beppu T. Cloning of the Membrane-Bound Aldehyde Dehydrogenase Gene of Acetobacter polyoxogenes and Improvement of Acetic Acid Production by Use of the Cloned Gene. Appl Environ Microbiol. 1989 Jan;55(1):171–176. [PMC free article] [PubMed]
  • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol. 1983 Jun 5;166(4):557–580. [PubMed]
  • Hanna Z, Fregeau C, Préfontaine G, Brousseau R. Construction of a family of universal expression plasmid vectors. Gene. 1984 Oct;30(1-3):247–250. [PubMed]
  • Heim R, Strehler EE. Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases. Gene. 1991 Mar 1;99(1):15–23. [PubMed]
  • Hempel J, Kaiser R, Jörnvall H. Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13–28. [PubMed]
  • Hempel J, von Bahr-Lindström H, Jörnvall H. Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme. Eur J Biochem. 1984 May 15;141(1):21–35. [PubMed]
  • Hohn B, Collins J. A small cosmid for efficient cloning of large DNA fragments. Gene. 1980 Nov;11(3-4):291–298. [PubMed]
  • Jendrossek D, Steinbüchel A, Schlegel HG. Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus. Eur J Biochem. 1987 Sep 15;167(3):541–548. [PubMed]
  • Jendrossek D, Steinbüchel A, Schlegel HG. Alcohol dehydrogenase gene from Alcaligenes eutrophus: subcloning, heterologous expression in Escherichia coli, sequencing, and location of Tn5 insertions. J Bacteriol. 1988 Nov;170(11):5248–5256. [PMC free article] [PubMed]
  • Johansson J, von Bahr-Lindström H, Jeck R, Woenckhaus C, Jörnvall H. Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme. Eur J Biochem. 1988 Mar 15;172(3):527–533. [PubMed]
  • Jorgensen RA, Rothstein SJ, Reznikoff WS. A restriction enzyme cleavage map of Tn5 and location of a region encoding neomycin resistance. Mol Gen Genet. 1979;177(1):65–72. [PubMed]
  • Knauf VC, Nester EW. Wide host range cloning vectors: a cosmid clone bank of an Agrobacterium Ti plasmid. Plasmid. 1982 Jul;8(1):45–54. [PubMed]
  • Kok M, Oldenhuis R, van der Linden MP, Meulenberg CH, Kingma J, Witholt B. The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. J Biol Chem. 1989 Apr 5;264(10):5442–5451. [PubMed]
  • Kustu S, Santero E, Keener J, Popham D, Weiss D. Expression of sigma 54 (ntrA)-dependent genes is probably united by a common mechanism. Microbiol Rev. 1989 Sep;53(3):367–376. [PMC free article] [PubMed]
  • López JM, Thoms B, Rehbein H. Acetoin degradation in Bacillus subtilis by direct oxidative cleavage. Eur J Biochem. 1975 Sep 15;57(2):425–430. [PubMed]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed]
  • O'Connell MJ, Kelly JM. Physical characterization of the aldehyde-dehydrogenase-encoding gene of Aspergillus niger. Gene. 1989 Dec 7;84(1):173–180. [PubMed]
  • Oppermann FB, Schmidt B, Steinbüchel A. Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J Bacteriol. 1991 Jan;173(2):757–767. [PMC free article] [PubMed]
  • Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem. 1989 Sep 15;264(26):15293–15297. [PubMed]
  • Pickett M, Gwynne DI, Buxton FP, Elliott R, Davies RW, Lockington RA, Scazzocchio C, Sealy-Lewis HM. Cloning and characterization of the aldA gene of Aspergillus nidulans. Gene. 1987;51(2-3):217–226. [PubMed]
  • Priefert H, Hein S, Krüger N, Zeh K, Schmidt B, Steinbüchel A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J Bacteriol. 1991 Jul;173(13):4056–4071. [PMC free article] [PubMed]
  • Reitzer LJ, Magasanik B. Expression of glnA in Escherichia coli is regulated at tandem promoters. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1979–1983. [PMC free article] [PubMed]
  • Römermann D, Warrelmann J, Bender RA, Friedrich B. An rpoN-like gene of Alcaligenes eutrophus and Pseudomonas facilis controls expression of diverse metabolic pathways, including hydrogen oxidation. J Bacteriol. 1989 Feb;171(2):1093–1099. [PMC free article] [PubMed]
  • Saigal D, Cunningham SJ, Farrés J, Weiner H. Molecular cloning of the mitochondrial aldehyde dehydrogenase gene of Saccharomyces cerevisiae by genetic complementation. J Bacteriol. 1991 May;173(10):3199–3208. [PMC free article] [PubMed]
  • Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. [PMC free article] [PubMed]
  • SCHLEGEL HG, KALTWASSER H, GOTTSCHALK G. [A submersion method for culture of hydrogen-oxidizing bacteria: growth physiological studies]. Arch Mikrobiol. 1961;38:209–222. [PubMed]
  • Strauss EC, Kobori JA, Siu G, Hood LE. Specific-primer-directed DNA sequencing. Anal Biochem. 1986 Apr;154(1):353–360. [PubMed]
  • Tamaki T, Horinouchi S, Fukaya M, Okumura H, Kawamura Y, Beppu T. Nucleotide sequence of the membrane-bound aldehyde dehydrogenase gene from Acetobacter polyoxogenes. J Biochem. 1989 Oct;106(4):541–544. [PubMed]
  • Tinoco I, Jr, Borer PN, Dengler B, Levin MD, Uhlenbeck OC, Crothers DM, Bralla J. Improved estimation of secondary structure in ribonucleic acids. Nat New Biol. 1973 Nov 14;246(150):40–41. [PubMed]
  • Tran-Betcke A, Warnecke U, Böcker C, Zaborosch C, Friedrich B. Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J Bacteriol. 1990 Jun;172(6):2920–2929. [PMC free article] [PubMed]
  • Vieira J, Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. [PubMed]
  • von Bahr-Lindström H, Hempel J, Jörnvall H. The cytoplasmic isoenzyme of horse liver aldehyde dehydrogenase. Relationship to the corresponding human isoenzyme. Eur J Biochem. 1984 May 15;141(1):37–42. [PubMed]
  • von Bahr-Lindström H, Jeck R, Woenckhaus C, Sohn S, Hempel J, Jörnvall H. Characterization of the coenzyme binding site of liver aldehyde dehydrogenase: differential reactivity of coenzyme analogues. Biochemistry. 1985 Oct 8;24(21):5847–5851. [PubMed]
  • Yoshida A, Huang IY, Ikawa M. Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258–261. [PMC free article] [PubMed]

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