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. 1989 Feb;171(2):1063–1067. doi: 10.1128/jb.171.2.1063-1067.1989

Modulation of alcohol dehydrogenase isoenzyme levels in Zymomonas mobilis by iron and zinc.

K F Mackenzie 1, C K Eddy 1, L O Ingram 1
PMCID: PMC209702  PMID: 2914864

Abstract

Zymomonas mobilis is an unusual microorganism which utilizes both iron-containing alcohol dehydrogenase (ADHII) and zinc-containing alcohol dehydrogenase (ADHI) isoenzymes during fermentative growth. This organism is obligately ethanologenic, and alcohol dehydrogenase activity is essential. The activities of ADHI and ADHII were altered by supplementing growth medium with iron or zinc salts and by iron starvation. Growth under iron-limiting conditions (chelators, minimal medium) reduced ADHII activity but did not prevent the synthesis of the ADHII protein. The inactive form of this enzyme appeared quite stable, was not renatured by iron addition, and persisted in the cell. The iron-induced increase in ADHII activity required de novo synthesis which was blocked by antibiotic additions. The ability of Z. mobilis to synthesize ADHII and ADHI may be advantageous in nature.

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Selected References

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  1. Bryant F. O., Wiegel J., Ljungdahl L. G. Purification and Properties of Primary and Secondary Alcohol Dehydrogenases from Thermoanaerobacter ethanolicus. Appl Environ Microbiol. 1988 Feb;54(2):460–465. doi: 10.1128/aem.54.2.460-465.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chang C., Meyerowitz E. M. Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1408–1412. doi: 10.1073/pnas.83.5.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Conway T., Sewell G. W., Osman Y. A., Ingram L. O. Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis. J Bacteriol. 1987 Jun;169(6):2591–2597. doi: 10.1128/jb.169.6.2591-2597.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ingram L. O., Conway T., Clark D. P., Sewell G. W., Preston J. F. Genetic engineering of ethanol production in Escherichia coli. Appl Environ Microbiol. 1987 Oct;53(10):2420–2425. doi: 10.1128/aem.53.10.2420-2425.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ingram L. O., Conway T. Expression of Different Levels of Ethanologenic Enzymes from Zymomonas mobilis in Recombinant Strains of Escherichia coli. Appl Environ Microbiol. 1988 Feb;54(2):397–404. doi: 10.1128/aem.54.2.397-404.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Langston-Unkefer P. J., Gander J. E. Occurrence of multiple forms of alcohol dehydrogenase in Penicillium supplemented with 2,3-butanediol. Arch Biochem Biophys. 1984 Sep;233(2):447–456. doi: 10.1016/0003-9861(84)90466-1. [DOI] [PubMed] [Google Scholar]
  8. Langston P. J., Pace C. N., Hart G. E. Wheat Alcohol Dehydrogenase Isozymes: PURIFICATION, CHARACTERIZATION, AND GENE EXPRESSION. Plant Physiol. 1980 Mar;65(3):518–522. doi: 10.1104/pp.65.3.518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Laurell C. B. Electroimmuno assay. Scand J Clin Lab Invest Suppl. 1972;124:21–37. doi: 10.3109/00365517209102748. [DOI] [PubMed] [Google Scholar]
  10. Leibold E. A., Munro H. N. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated region of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2171–2175. doi: 10.1073/pnas.85.7.2171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Luria S. E., Delbrück M. Mutations of Bacteria from Virus Sensitivity to Virus Resistance. Genetics. 1943 Nov;28(6):491–511. doi: 10.1093/genetics/28.6.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lutstorf U., Megnet R. Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae. I. Physiological control of ADH-2 and properties of ADH-2 and ADH-4. Arch Biochem Biophys. 1968 Sep 10;126(3):933–944. doi: 10.1016/0003-9861(68)90487-6. [DOI] [PubMed] [Google Scholar]
  13. Neale A. D., Scopes R. K., Kelly J. M., Wettenhall R. E. The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles. Eur J Biochem. 1986 Jan 2;154(1):119–124. doi: 10.1111/j.1432-1033.1986.tb09366.x. [DOI] [PubMed] [Google Scholar]
  14. Scopes R. K. An iron-activated alcohol dehydrogenase. FEBS Lett. 1983 Jun 13;156(2):303–306. doi: 10.1016/0014-5793(83)80517-1. [DOI] [PubMed] [Google Scholar]
  15. Williamson V. M., Paquin C. E. Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis. Mol Gen Genet. 1987 Sep;209(2):374–381. doi: 10.1007/BF00329668. [DOI] [PubMed] [Google Scholar]
  16. Wills C., Kratofil P., Londo D., Martin T. Characterization of the two alcohol dehydrogenases of Zymomonas mobilis. Arch Biochem Biophys. 1981 Sep;210(2):775–785. doi: 10.1016/0003-9861(81)90245-9. [DOI] [PubMed] [Google Scholar]
  17. Young E. T., Pilgrim D. Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol. 1985 Nov;5(11):3024–3034. doi: 10.1128/mcb.5.11.3024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Youngleson Jonathan S., Santangelo Joseph D., Jones David T., Woods David R. Cloning and Expression of a Clostridium acetobutylicum Alcohol Dehydrogenase Gene in Escherichia coli. Appl Environ Microbiol. 1988 Mar;54(3):676–682. doi: 10.1128/aem.54.3.676-682.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]

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