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Neurospora glucamylase and a mutant affected in its regulation

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Abstract

Neurospora glucamylase is a glucose-repressible extracellular enzyme. The enzyme was purified to homogeneity and found to have a molecular weight of 82,000 and to release glucose from either maltose or amylose. The rate of glucamylase synthesis increases more than 100-fold when cells are transferred from a glucose-containing medium to a glucose-free medium. Increased production of glucamylase begins within 30 min of the transfer. Glucamylase is rapidly secreted into the medium. A mutant affecting the ability of glucose to repress the synthesis of the glucose-repressible extracellular enzymes glucamylase and invertase has been isolated and studied. The mutant constitutively synthesizes and secretes a glucamylase which is indistinguishable from the wild-type enzyme.

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References

  • Carlson, M., and Botstein, D. (1982). Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28145.

    Google Scholar 

  • Carlson, M., Osmond, B. C., and Botstein, D. (1981). Mutants of yeast defective in sucrose utilization. Genetics 9825.

    Google Scholar 

  • Davis, R. H., and DeSerres, F. J. (1970). Genetic and Microbiological research techniques for Neurospora crassa. Methods Enzymol. 1779.

    Google Scholar 

  • Eggerding, C., Randall, J. A., and Sargent, M. L. (1975). An altered invertase in the cot-2 mutant of Neurospora crassa. J. Gen. Microbiol. 89102.

    Google Scholar 

  • Elorza, M. V., Villanueva, J. R., and Sentandreu, R. (1977). The mechanism of catabolite inhibition of invertase by glucose in Saccharomyces cerevesiae. Biochim. Biophys. Acta 4751093.

    Google Scholar 

  • Federoff, H. J., Eccleshall, T. R., and Marmur, J. (1983). Carbon catabolite repression of maltase synthesis in Saccharomyces carlsbergensis. J. Bacteriol. 156301.

    Google Scholar 

  • Free, S. J., and Metzenberg, R. L. (1982). The synthesis of alkaline phosphatase in Neurospora crassa. Biochem. Genet. 20883.

    Google Scholar 

  • Gabriel, O., and Wang, S.-F. (1969). Determination of enzymatic activity in polyacrylamide gels. I. Enzymes catalyzing the conversion of non-reducing substrates to reducing products. Anal. Biochem. 27545.

    Google Scholar 

  • Gascon, S., and Lampen, J. O. (1968). Purification of the internal invertase of Yeast. J. Biol. Chem. 2431567.

    Google Scholar 

  • Gratzner, H. G. (1972). Cell wall alterations associated with the hyperproduction of extracellular enzymes in Neurospora crassa. J. Bacteriol. 111443.

    Google Scholar 

  • Hynes, M. J., and Kelly, J. M. (1977). Pleiotropic mutants of Aspergillus nidulans altered in carbon metabolism. Mol. Gen. Genet. 150193.

    Google Scholar 

  • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227680.

    Google Scholar 

  • Lee, D. B., and Free, S. J. (1984). The isolation and characterization of Neurospora mutants affected in invertase synthesis. Genetics 106591.

    Google Scholar 

  • Lineback, D. R., Russell, I. J., and Rasmussen, C. (1969). Two forms of the glucamylase of Aspergillus niger. Arch. Biochem. Biophys. 134539.

    Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with Folin phenol reagent. J. Biol. Chem. 193265.

    Google Scholar 

  • Metzenberg, R. L. (1979). Implications of some genetic control mechanisms in Neurospora. Microbiol. Rev. 43361.

    Google Scholar 

  • Montecourt, B. S., Kuo, S.-C., and Lampen, J. O. (1973). Saccharomyces mutants with invertase formation resistant to repression by hexoses. J. Bacteriol. 114233.

    Google Scholar 

  • Murayama, T., and Ishikawa, T. (1973). Mutation in Neurospora crassa affecting some of the extracellular enzymes and several growth characteristics. J. Bacteriol. 115796.

    Google Scholar 

  • Street, H. V. (1974). Measurement of starch-iodine complex. In Bergmeyer, H. U. (ed.), Methods of Enzymatic Analysis, Vol. 2, pp. 898–903.

  • Takahashi, T., Inokuchi, N., and Irie, M. (1981). Purification and characterization of a glucamylase from Aspergillus saitori. J. Biochem. 89125.

    Google Scholar 

  • Trevithick, J. R., and Metzenberg, R. L. (1966). Molecular sieving by Neurospora cell walls during secretion of invertase isozymes. J. Bacteriol. 921010.

    Google Scholar 

  • Yamasaki, Y., Suzuki, Y., and Ozawa, J. (1977a). Purification and properties of two forms of glucamylase from Pencillium oxalicum. Agr. Biol. Chem. 41755.

    Google Scholar 

  • Yamasaki, Y., Suzuki, Y., and Ozawa, J. (1977b). Three forms of a-glucosidase and a-glucamylase from Aspergillus awamori. Agr. Biol. Chem. 412149.

    Google Scholar 

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Funds for this research were provided by Grant PCM-8011772 from the National Science Foundation and by a grant from the Research Development Fund of The Research Foundation of the State University of New York.

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Sigmund, R.D., McNally, M.T., Lee, D.B. et al. Neurospora glucamylase and a mutant affected in its regulation. Biochem Genet 23, 89–103 (1985). https://doi.org/10.1007/BF00499115

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  • DOI: https://doi.org/10.1007/BF00499115

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