Abstract
Two complementing loci in different linkage groups of the basidiomycete Ustilago violacea are involved in urease activity: a structural one (ure-1) and a second inferred to involve a permease (ure-2) locus. Two types of complementing mutations occur in the structural locus: null activity (ure-1a) and obviously reduced activity (ure-1b). The ure-2 mutants lacked urease activity in vivo on the phenol red-urea test medium, but gave extracts with wild-type activity. Extracts from wild-type strains gave one site of urease activity after polyacrylamide gel electrophoresis. A number of ure-1b mutants and active revertants from ure-1a mutants yielded electrophoretically variant urease sites. The results are discussed in terms of enzyme polymorphism in haploid eukaryotes by one (missense) or two (null, then missense) mutations.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Baird, M. L., and Garber, E. D. (1979). Genetics of Ustilago violacea. IV. An electrophoretic survey for urease variants in wild strains. Bot. Gaz. 14084.
Benson, E. W., and Howe, H. B., Jr. (1978). Reversion and interallelic complementation at four urease loci in Neurospora crassa. Mol. Gen. Genet. 165277.
Bradford, L. S., Jones, R. J., and Garber, E. D. (1975). An electrophoretic survey of fourteen species of the fungal genus Ustilago. Bot. Gaz. 136109.
Christensen, W. B. (1946). Urea decomposition as a means of differentiating Proteus and Paracolon cultures from each other and from Salmonella and Shigella types. J. Bact. 52461.
Clare, B. G., Flentje, N. T., and Atkinson, M. R. (1968). Electrophoretic patterns of oxidoreductases and other proteins as criteria in fungal taxonomy. Austral. J. Sci. 21275.
Cooper, T. G., and Sumrada, R. (1975). Urea transport in Saccharomyces cerevisiae. J. Bact. 121571.
Davis, R. H. (1970). Sources of urea in Neurospora. Biochim. Biophys. Acta 251412.
Day, A. W., and Jones, J. K. (1968). The production and characterization of diploids in Ustilago violacea. Genet. Res. 1163.
Day, A. W., and Jones, J. K. (1969). Sexual and parasexual analysis of Ustilago violacea. Genet. Res. 14195.
Fishbein, W. N., Winter, T. S., and Dividson, J. D. (1965). Urease catalysis. I. Stoichiometry, specificity, and kinetics of a second substrate: Hydroxyurea. J. Biol. Chem. 2402402.
Fishbein, W. N. (1969). The structural basis for the catalytic complexity of urease: Interacting and interconvertible molecular species (with a note on isozyme classes). N.Y. Acad. Sci. 147857.
Gorin, G., and Chin, C. C. (1966). Urease. VI. A new method of assay and the specific enzymatic activity. Anal. Biochem. 1749.
Haysman, P., and Howe, H. B. (1971). Some genetic and physiological characteristics of urease-defective strains of Neurospora crassa. Can. J. Gen. Cytol. 13256.
Hubby, H. L., and Lewontin, R. C. (1966). A molecular approach to the study of genic heterozygosity in natural populations. I. The number of alleles at different loci in Drosophila psuedoobscura. Genetics 54577.
Kurzeja, K. C., and Garber, E. D. (1973). A genetic study of electrophoretically variant extracellular amylotic enzymes of wild-type strains of Aspergillus nidulans. Can. J. Genet. Cytol. 15275.
Larson, K. J., and Kallio, R. E. (1954). Purification and properties of bacterial urease. J. Bact. 6867.
Leob, W. F., and Stuhlman, R. A. (1969). A colorimetric method for the determination of serum arginase activity. Clin. Chem. 15152.
Reithel, F. J., Robbins, J. E., and Gorin, G. (1964). A structural subunit molecular weight of urease. Arch. Biochem. 108409.
Roon, R. J., and Levenberg, B. (1972). Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 2474107.
Siegel, L. M., and Monty, K. J. (1965). Determination of molecular weights and frictional ratios of macromolecules in impure systems: Aggregation of urease. Biochem. Biophys. Res. Commun. 19494.
Sumner, J. B. (1926). The isolation and crystallization of the enzyme urease. J. Biol. Chem. 69435.
Summer, J. B., Graten, N., and Erikson-Quensel, I. (1938). The molecular weight of urease. J. Biol. Chem. 12537.
West, N. B., and Garber, E. D. (1967). Genetic studies of variant enzymes. I. An electrophoretic survey of esterases and leucine aminopeptidases in the genus Phaseolus. Can. J. Genet. Cytol. 9640.
Whitney, P. A., and Cooper, T. G. (1972). Urea carboxylase and allophanate hydrolase. Two components of adenosine triphosphate: Urea and lyase in Saccharomyces cerevisiae. J. Biol. Chem. 2471349.
Author information
Authors and Affiliations
Additional information
We acknowledge financial support from the Louis Block Fund of the University of Chicago to E. D. Garber and Cellular Biology Training Grant PHS-HD-00174 and Genetics and Regulation Training Grants GM-07197 and PHS-GM-1797-02 to M. L. Baird.
Rights and permissions
About this article
Cite this article
Baird, M.L., Garber, E.D. The genetics and biochemistry of urease in Ustilago violacea . Biochem Genet 19, 1101–1114 (1981). https://doi.org/10.1007/BF00484568
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484568