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. 1989 May;171(5):2646–2652. doi: 10.1128/jb.171.5.2646-2652.1989

Evidence for three differentially regulated catalase genes in Neurospora crassa: effects of oxidative stress, heat shock, and development.

P Chary 1, D O Natvig 1
PMCID: PMC209947  PMID: 2540152

Abstract

Genetic and biochemical studies demonstrated that Neurospora crassa possesses three catalases encoded by three separate structural genes. The specific activities of the three enzymes varied in response to superoxide-mediated stress, heat shock, and development. The three loci, which we designated cat-1, cat-2, and cat-3, map to the right arms of chromosomes III, VII, and III, respectively. The cat-1-encoded enzyme (designated Cat-1; estimated molecular weight, 315,000; pI 5.2) was the predominant catalase in rapid-growth mycelium, and its activity was substantially increased in paraquat-treated and heat-shocked mycelium. Cat-2 (Mw, 165,000; pI 5.4) was absent from rapid-growth mycelium but present at low levels in conidia and stationary-phase mycelium. It was the predominant catalase in extracts derived from mycelium that had been heat shocked for 2 h. Cat-3 (Mw, 340,000; pI 5.5) was the predominant catalase in extracts from mature conidia.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [PubMed] [Google Scholar]
  2. Bewley G. C., Mackay W. J., Cook J. L. Temporal variation for the expression of catalase in Drosophila melanogaster: correlations between rates of enzyme synthesis and levels of translatable catalase-messenger RNA. Genetics. 1986 Aug;113(4):919–938. doi: 10.1093/genetics/113.4.919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brawn K., Fridovich I. DNA strand scission by enzymically generated oxygen radicals. Arch Biochem Biophys. 1981 Feb;206(2):414–419. doi: 10.1016/0003-9861(81)90108-9. [DOI] [PubMed] [Google Scholar]
  4. Bray R. C., Cockle S. A., Fielden E. M., Roberts P. B., Rotilio G., Calabrese L. Reduction and inactivation of superoxide dismutase by hydrogen peroxide. Biochem J. 1974 Apr;139(1):43–48. doi: 10.1042/bj1390043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brennan T., Frenkel C. Involvement of hydrogen peroxide in the regulation of senescence in pear. Plant Physiol. 1977 Mar;59(3):411–416. doi: 10.1104/pp.59.3.411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chandlee J. M., Scandalios J. G. Regulation of Cat1 gene expression in the scutellum of maize during early sporophytic development. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4903–4907. doi: 10.1073/pnas.81.15.4903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Christman M. F., Morgan R. W., Jacobson F. S., Ames B. N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 1985 Jul;41(3):753–762. doi: 10.1016/s0092-8674(85)80056-8. [DOI] [PubMed] [Google Scholar]
  8. Fridovich I. Superoxide dismutases. Annu Rev Biochem. 1975;44:147–159. doi: 10.1146/annurev.bi.44.070175.001051. [DOI] [PubMed] [Google Scholar]
  9. Halliwell B. Biochemical mechanisms accounting for the toxic action of oxygen on living organisms: the key role of superoxide dismutase. Cell Biol Int Rep. 1978 Mar;2(2):113–128. doi: 10.1016/0309-1651(78)90032-2. [DOI] [PubMed] [Google Scholar]
  10. Hassan H. M., Fridovich I. Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch Biochem Biophys. 1979 Sep;196(2):385–395. doi: 10.1016/0003-9861(79)90289-3. [DOI] [PubMed] [Google Scholar]
  11. Hayes M. B., Wellner D. Microheterogeneity of L-amino acid oxidase. Separation of multiple components by polyacrylamide gel electrofucusing. J Biol Chem. 1969 Dec 25;244(24):6636–6644. [PubMed] [Google Scholar]
  12. Hedrick J. L., Smith A. J. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys. 1968 Jul;126(1):155–164. doi: 10.1016/0003-9861(68)90569-9. [DOI] [PubMed] [Google Scholar]
  13. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 1975 Dec 2;14(24):5294–5299. doi: 10.1021/bi00695a010. [DOI] [PubMed] [Google Scholar]
  14. Jacob G. S., Orme-Johnson W. H. Catalase of Neurospora crassa. 1. Induction, purification, and physical properties. Biochemistry. 1979 Jul 10;18(14):2967–2975. doi: 10.1021/bi00581a009. [DOI] [PubMed] [Google Scholar]
  15. Lee P. C., Bochner B. R., Ames B. N. AppppA, heat-shock stress, and cell oxidation. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7496–7500. doi: 10.1073/pnas.80.24.7496. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Loewen P. C., Switala J. Multiple catalases in Bacillus subtilis. J Bacteriol. 1987 Aug;169(8):3601–3607. doi: 10.1128/jb.169.8.3601-3607.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Loewen P. C., Switala J., Triggs-Raine B. L. Catalases HPI and HPII in Escherichia coli are induced independently. Arch Biochem Biophys. 1985 Nov 15;243(1):144–149. doi: 10.1016/0003-9861(85)90782-9. [DOI] [PubMed] [Google Scholar]
  18. Morgan R. W., Christman M. F., Jacobson F. S., Storz G., Ames B. N. Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8059–8063. doi: 10.1073/pnas.83.21.8059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Morrissey J. H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem. 1981 Nov 1;117(2):307–310. doi: 10.1016/0003-2697(81)90783-1. [DOI] [PubMed] [Google Scholar]
  20. Munkres K. D., Rana R. S., Goldstein E. Genetically determined conidial longevity is positively correlated with superoxide dismutase, catalase, glutathione peroxidase, cytochrome c peroxidase, and ascorbate free radical reductase activities in Neurospora crassa. Mech Ageing Dev. 1984 Jan;24(1):83–100. doi: 10.1016/0047-6374(84)90177-5. [DOI] [PubMed] [Google Scholar]
  21. Privalle C. T., Fridovich I. Induction of superoxide dismutase in Escherichia coli by heat shock. Proc Natl Acad Sci U S A. 1987 May;84(9):2723–2726. doi: 10.1073/pnas.84.9.2723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Righetti P. G., Gianazza E. Isoelectric focusing of heparin. Evidence for complexing with carrier ampholytes. Biochim Biophys Acta. 1978 Jan 25;532(1):137–146. doi: 10.1016/0005-2795(78)90456-7. [DOI] [PubMed] [Google Scholar]
  23. Rowley D. A., Halliwell B. DNA damage by superoxide-generating systems in relation to the mechanism of action of the anti-tumour antibiotic adriamycin. Biochim Biophys Acta. 1983 Nov 22;761(1):86–93. doi: 10.1016/0304-4165(83)90365-3. [DOI] [PubMed] [Google Scholar]
  24. Sammartano L. J., Tuveson R. W., Davenport R. Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus. J Bacteriol. 1986 Oct;168(1):13–21. doi: 10.1128/jb.168.1.13-21.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sammartano L. J., Tuveson R. W. The effects of exogenous catalase on broad-spectrum near-UV (300-400 nm) treated Escherichia coli cells. Photochem Photobiol. 1984 Nov;40(5):607–612. doi: 10.1111/j.1751-1097.1984.tb05348.x. [DOI] [PubMed] [Google Scholar]
  26. Shimizu M., Egashira T., Takahama U. Inactivation of Neurospora crassa conidia by singlet molecular oxygen generated by a photosensitized reaction. J Bacteriol. 1979 May;138(2):293–296. doi: 10.1128/jb.138.2.293-296.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Takahama U., Shimizu-Takahama M., Egashira T. Reduction of exogenous cytochrome c by Neurospora crassa conidia: effects of superoxide dismutase and blue light. J Bacteriol. 1982 Oct;152(1):151–156. doi: 10.1128/jb.152.1.151-156.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Thomas S. A., Sargent M. L., Tuveson R. W. Inactivation of normal and mutant Neurospora crassa conidia by visible light and near-UV: role of 1O2, carotenoid composition and sensitizer location. Photochem Photobiol. 1981 Mar;33(3):349–354. doi: 10.1111/j.1751-1097.1981.tb05428.x. [DOI] [PubMed] [Google Scholar]

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