1887

Abstract

Aldo-keto reductases (AKRs) are a superfamily of enzymes that reduce aldehydes and ketones, and have a broad range of substrates. An AKR gene, , was identified in the cyanobacterium sp. PCC 7002. A mutant strain with inactivated was sensitive to glycerol, a carbon source that can support heterotrophic growth of sp. PCC 7002. It was found that the null mutant accumulated more toxic methylglyoxal than the wild-type when glycerol was added to growth medium, suggesting that SakR1 is involved in the detoxification of methylglyoxal, a highly toxic metabolite that can damage cellular macromolecules. Enzymic analysis of recombinant SakR1 protein showed that it can efficiently reduce methylglyoxal with NADPH. Based on immunoblotting, SakR1 was not upregulated at an increased cellular methylglyoxal concentration. A pH-dependent enzyme-activity profile suggested that SakR1 activity could be regulated by cellular pH in sp. PCC 7002. The broad substrate specificity of SakR1 implies that SakR1 could play other roles in cellular metabolism.

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2006-07-01
2019-11-21
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References

  1. Baskaran, S., Prasanna Rajan, D. & Balasubranmanian, K. A. ( 1989; ). Formation of methylglyoxal by bacteria isolated from human faeces. J Med Microbiol 28, 211–215.[CrossRef]
    [Google Scholar]
  2. Blattner, F. R., Plunkett, G., III, Bloch, C. A. & 14 other authors ( 1997; ). The complete genome sequence of Escherichia coli K-12. Science 277, 1453–1474.[CrossRef]
    [Google Scholar]
  3. Booth, I. R., Ferguson, G. P., Miller, S., Li, C., Gunasekera, B. & Kinghorn, S. ( 2003; ). Bacterial production of methylglyoxal: a survival strategy or death by misadventure? Biochem Soc Trans 31, 1406–1408.[CrossRef]
    [Google Scholar]
  4. Burke, R. M. & Tempest, D. W. ( 1990; ). Growth of Bacillus stearothermophilus on glycerol in chemostat culture: expression of an unusual phenotype. J Gen Microbiol 136, 1381–1385.[CrossRef]
    [Google Scholar]
  5. Buzby, J. S., Porter, R. D. & Stevens, S. E., Jr ( 1985; ). Expression of the Escherichia coli lacZ gene on a plasmid vector in a cyanobacterium. Science 230, 805–807.[CrossRef]
    [Google Scholar]
  6. Cordeiro, C. & Freire, P. A. ( 1996; ). Methylglyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent. Anal Biochem 234, 221–224.[CrossRef]
    [Google Scholar]
  7. Ellis, E. M. ( 2002; ). Microbial aldo-keto reductases. FEMS Microbiol Lett 216, 123–131.[CrossRef]
    [Google Scholar]
  8. Ellis, E. M., Judah, D. J., Neal, G. E. & Hayes, J. D. ( 1993; ). An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases. Proc Natl Acad Sci U S A 90, 10350–10354.[CrossRef]
    [Google Scholar]
  9. Ferguson, G. P., Totemeyer, S., Maclean, M. J. & Booth, I. R. ( 1998; ). Methylglyoxal production in bacteria: suicide or survival? Arch Microbiol 170, 209–219.[CrossRef]
    [Google Scholar]
  10. Freedberg, W. B., Kistler, W. S. & Lin, E. C. C. ( 1971; ). Lethal synthesis of methylglyoxal by Escherichia coli during unregulated glycerol metabolism. J Bacteriol 108, 137–144.
    [Google Scholar]
  11. Goffeau, A., Barrell, B. G., Bussey, H. & 13 other authors ( 1996; ). Life with 6000 genes. Science 274, 546–567.[CrossRef]
    [Google Scholar]
  12. Grant, A. W., Steel, G., Waugh, H. & Ellis, E. M. ( 2003; ). A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity. FEMS Microbiol Lett 218, 93–99.[CrossRef]
    [Google Scholar]
  13. Hinshelwood, A., MaGarvie, G. & Ellis, E. M. ( 2002; ). Characterization of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett 523, 213–218.[CrossRef]
    [Google Scholar]
  14. Hopper, D. J. & Cooper, R. A. ( 1971; ). The regulation of Escherichia coli methylglyoxal synthase: a new control of glycolysis. FEBS Lett 13, 213–216.[CrossRef]
    [Google Scholar]
  15. Inoue, Y. & Kimmura, A. ( 1995; ). Methylglyoxal and regulation of its metabolism in microorganisms. Adv Microb Physiol 37, 177–227.
    [Google Scholar]
  16. Jez, J. M. & Penning, T. M. ( 2001; ). The also-keto reductase (AKR) superfamily: an update. Chem Biol Interact 130–132, 499–525.
    [Google Scholar]
  17. Jez, J. M., Bennett, M. J., Schlegel, B. P., Lewis, M. & Penning, T. M. ( 1997; ). Comparative anatomy of the aldo-keto reductase superfamily. Biochem J 326, 625–636.
    [Google Scholar]
  18. Kalapos, M. P. ( 1999; ). Methylglyoxal in living organisms. Chemistry, biochemistry, toxicology and biological implications. Toxicol Lett 110, 145–175.[CrossRef]
    [Google Scholar]
  19. Kim, I., Kim, E., Yoo, S., Shin, D., Min, B., Song, J. & Park, C. ( 2004; ). Ribose utilization with an excess of mutarotase causes cell death due to accumulation of methylglyoxal. J Bacteriol 186, 7229–7235.[CrossRef]
    [Google Scholar]
  20. Ko, J., Kim, I., Yoo, S., Min, B., Kim, K. & Park, C. ( 2005; ). Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases. J Bacteriol 187, 5782–5789.[CrossRef]
    [Google Scholar]
  21. Kunst, F., Ogasawara, N., Moszer, I. & 148 other authors ( 1997; ). The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390, 249–256.[CrossRef]
    [Google Scholar]
  22. Laemmli, U. K. ( 1970; ). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.[CrossRef]
    [Google Scholar]
  23. MacKinney, G. ( 1941; ). Absorption of light by chlorophyll solutions. J Biol Chem 140, 315–322.
    [Google Scholar]
  24. O'Connor, T., Ireland, L. S., Harrison, D. J. & Hayes, J. D. ( 1999; ). Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J 343, 487–504.[CrossRef]
    [Google Scholar]
  25. Peterson, G. L. ( 1974; ). A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83, 346–356.
    [Google Scholar]
  26. Phillips, S. A. & Thornalley, P. J. ( 1993; ). The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal. Eur J Biochem 212, 101–105.[CrossRef]
    [Google Scholar]
  27. Rippka, R., Deruelles, J., Waterbury, J. B., Herdman, M. & Stanier, R. Y. ( 1979; ). Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J Gen Microbiol 111, 1–61.[CrossRef]
    [Google Scholar]
  28. Russel, J. B. ( 1993; ). Glucose toxicity in Prevotella ruminicola: methylglyoxal accumulation and its effect on membrane physiology. Appl Environ Microbiol 59, 2844–2850.
    [Google Scholar]
  29. Russell, J. B. & Cook, G. M. ( 1995; ). Energetics of bacterial growth: balance of anabolic and catabolic reactions. Microbiol Rev 59, 48–62.
    [Google Scholar]
  30. Stevens, S. E., Jr, Patterson, C. O. P. & Myers, J. ( 1973; ). The production of hydrogen peroxide by blue-green algae: a survey. J Phycol 9, 427–430.
    [Google Scholar]
  31. Tempest, D. W. & Neijssel, O. M. ( 1984; ). The status of YATP and maintenance energy as biologically interpretable phenomena. Annu Rev Microbiol 38, 459–486.[CrossRef]
    [Google Scholar]
  32. Thompson, J. D., Higgins, D. G. & Gibson, T. J. ( 1994; ). clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673–4680.[CrossRef]
    [Google Scholar]
  33. Wermuth, B., Munch, J. D. & von Wartburg, J. P. ( 1977; ). Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 252, 3821–3828.
    [Google Scholar]
  34. Xu, D., Liu, X., Zhao, J. & Zhao, J. ( 2005; ). FesM, a membrane iron-sulfur protein, is required for cyclic electron flow around photosystem I and photoheterotrophic growth of the cyanobacterium Synechococcus sp. PCC 7002. Plant Physiol 138, 1586–1595.[CrossRef]
    [Google Scholar]
  35. Zhao, J., Shen, G. & Bryant, D. A. ( 2001; ). Photosystem stoichiometry and state transitions in a mutant of the cyanobacterium Synechococcus sp. PCC 7002 lacking phycocyanin. Biochim Biophys Acta 1505, 248–257.[CrossRef]
    [Google Scholar]
  36. Zhou, R., Cao, Z. & Zhao, J. ( 1998; ). Characterization of HetR protein turnover in Anabaena sp. PCC 7120. Arch Microbiol 169, 417–423.[CrossRef]
    [Google Scholar]
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