Abstract
Results of a cross between a hyperderepressed strain (89601 a) and a normal strain (74A) of Neurospora crassa suggest that there is a single gene difference in this trait. The evidence is clearest with amylase although a similar segregation pattern is suggested for invertase and, perhaps, trehalase. On the other hand, phosphatase activity is not affected by this gene. The gene for hyperderepression does not appear to be widespread in wild-type strains of this organism for, in the seven tested, only 89601 a was hyperderepressed for amylase. The action of the hyperderepression gene probably is not due to diminished sensitivity to catabolite repression because the synthesis of amylase begins at roughly the same point in glucose depletion in both the hyperderepressed and normal strains. Furthermore, growth of these strains on constant but low levels of a carbon source causes derepression to the degree expected in both strains. Nor does hyperderepression appear to be due to achange in sensitivity to induction, according to experiments with cellobiase, which is inducible. Increases in enzyme activity due to the gene for hyperderepression are in the order, amylase-cellobiase>invertase>trehalase. Thus, the gene exhibits polarity as well as being pleiotropic. An explanation for its effect is proposed, based upon changes in the cell surface.
Similar content being viewed by others
References
Anonymous: Techniques for high resolution electrophoresis. Ortec Application Note, AN 32. Oak Ridge, Tenn.: Ortec 1970
Bergmeyer, H. U.: Methods of enzymatic analysis. New York: Academic Press 1963
Bigger, C. H., White, M. R., Braymer, H. D.: Ultrastructure and invertase secretion of the slime mutant of Neurospora crassa. J. gen. Microbiol. 71, 159–166 (1972)
Bretscher, M.: Major human erythrocyte glycoprotein spans the cell membrane. Nature New Biol. 231, 229–232 (1971)
Calonge, F. D., Fielding, A. H., Byrde, R. J. W.: Multivesicular bodies in Sclerotinia fructigena and their possible relation to extracellular enzyme secretion. J. gen. Microbiol. 55, 117–184 (1969)
Chang, P. L.-Y.: Invertase and other exoenzymes in Neurospora. Ph. D. Dissertation, University of Western Ontario, London, Canada (1971)
Eberhart, B. M., Beck, R. S.: B-glucosidases in Neurospora tetrasperma. J. Bact. 101, 408–417 (1970)
Eberhart, B. M., Beck, R. S.: Induction of B-glucosidases in Neurospora tetrasperma. J. Bact. 116, 295–303 (1973)
Eilers, F. I., Allen, J., Hill, E. P., Sussman, A. S.: Localization of disaccharides in extracts of Neurospora after electrophoresis in polyacrylamide gels. J. Histochem. Cytochem. 12, 448–450 (1964)
Gingell, D.: Membrane permeability change by aggregation of mobile glycoprotein units. J. theor. Biol. 38, 677–679 (1973)
Gratzner, H. G.: Cell wall alterations associated with the hyperproduction of extracellular enzymes in Neurospora crassa. J. Bact. 111, 443–446 (1972)
Gratzner, H., Fass, D. N.: Report on the Fourth Neurospora Information Conference. Neurospora Newsletter 13, 10 (1968)
Gratzner, H., Sheehan, D. N.: Neurospora mutant exhibiting hyperproduction of amylase and invertase. J. Bact. 97, 544–549 (1969)
Harwood, J., Smith, D. H.: Catabolite repression of chloramphenicol acetyl transferase synthesis in E. coli K 12. Biochem. biophys. Res. Commun. 42, 57–62 (1971)
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, A. J.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951)
Metzenberg, R. L.: Enzymatically active subunits of Neurospora invertase. Biochim. biophys. Acta (Amst.) 77, 455–465 (1964)
Murayama, T., Ishikawa, T.: Mutation in Neurospora crassa affecting some of the extracellular enzymes and several growth characteristics. J. Bact. 115, 796–804 (1973)
Nakazawa, A., Tamada, T.: Stimulation of colicin E synthesis by cAMP in mitomycin C-induced E. coli. Biochem. biophys. Res. Commun. 46, 1004–1010 (1972)
Reese, E. T., Maguire, A.: Increase in cellulase yields by addition of surfactants to cellobiose cultures of Trichoderma viride. Chap. 24 in Develop. in Indust. Microbiol. 12, 212–224 (1971)
Somogyi, M.: Notes on sugar determination. J. biol. Chem. 195, 19–23 (1952)
Trevithick, J. R., Metzenberg, R. L.: Molecular sieving by Neurospora cell walls during secretion of invertase isozymes. J. Bact. 92, 1010–1015 (1966)
Vogel, H. J.: A convenient growth medium for Neurospora (Medium N). Microbiol. Genet. Bull. 13, 42–43 (1956)
Winkler, V., Timmis, K.: Pleiotropic mutations in Serratia marcescens which increase the synthesis of certain exocellular proteins and the rate of spontaneous prophage induction. Molec. Gen. Genet. 124, 197–206 (1973)
Yoneda, Y., Yamane, K., Marro, B.: Membrane mutation related to the production of extracellular α-amylase and protease in Bacillus subtilis. Biochem. biophys. Res. Commun. 50, 765–770 (1973)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Sternberg, D., Sussman, A.S. Hyperproduction of some glycosidases in Neurospora crassa . Arch. Microbiol. 101, 303–320 (1974). https://doi.org/10.1007/BF00455947
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00455947