Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1971 Oct;108(1):59–68. doi: 10.1128/jb.108.1.59-68.1971

Isolation, Mapping, and Characterization of Trehalaseless Mutants of Neurospora crassa

Alfred S Sussman a, M Kerry Garrett a, Malcolm Sargent a,1, Shih-An Yu a,2
PMCID: PMC247032  PMID: 5001211

Abstract

Mutant strains of Neurospora crassa that lack trehalase and are unable to grow on trehalose were isolated, and the gene (tre) was positioned on the right arm of linkage group I. Maltase and β-galactosidase activities are almost identical in tre− strains, whereas that of invertase was reduced by more than half and those of acid phosphatase and amylase were somewhat increased. Heterocaryons between standard and trehalaseless strains yield less than one-tenth the activity of the former. In addition, strains with duplications heterozygous for trehalase produce less than 1% of the activity of the standard strain. An inhibitor of trehalase has been found in tre− strains; its sensitivity to heat and proteolysis, and its nondialyzability suggest that this substance is a protein. The mig gene, which determines the rate of migration of trehalase on acrylamide gels, has been shown to be less than 1 map unit away from the tre gene.

Full text

PDF
60

Images in this article

64Image
on p.64

Selected References

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

  1. Davis R. H. Carbamyl phosphate synthesis in Neurospora crassa. II. Genetics, metabolic position, and regulation of arginine-specific carbamyl phosphokinase. Biochim Biophys Acta. 1965 Aug 24;107(1):54–68. doi: 10.1016/0304-4165(65)90388-0. [DOI] [PubMed] [Google Scholar]
  2. Davis R. H., Lawless M. B., Port L. A. Arginaseless Neurospora: genetics, physiology, and polyamine synthesis. J Bacteriol. 1970 May;102(2):299–305. doi: 10.1128/jb.102.2.299-305.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Davis R. H., Mora J. Mutants of Neurospora crassa deficient in ornithine-delta-transmainase. J Bacteriol. 1968 Aug;96(2):383–388. doi: 10.1128/jb.96.2.383-388.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Efron Y., Schwartz D. In vivo inactivation of maize alcohol dehydrogenase by a two-factor system. Proc Natl Acad Sci U S A. 1968 Oct;61(2):586–591. doi: 10.1073/pnas.61.2.586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GEORGATSOS J. G. ACID PHOSPHATASES OF HUMAN ERYTHROCYTES. Arch Biochem Biophys. 1965 May;110:354–356. doi: 10.1016/0003-9861(65)90133-5. [DOI] [PubMed] [Google Scholar]
  6. GIBSON Q. H., SWOBODA B. E., MASSEY V. KINETICS AND MECHANISM OF ACTION OF GLUCOSE OXIDASE. J Biol Chem. 1964 Nov;239:3927–3934. [PubMed] [Google Scholar]
  7. Gilby A. R., Wyatt S. S., Wyatt G. R. Trehalases from the cockroach, Blaberus discoidalis: activation, solubilization and properties of the muscle enzyme and some properties of the intestinal enzyme. Acta Biochim Pol. 1967;14(1):83–100. [PubMed] [Google Scholar]
  8. HILL E. P., SUSSMAN A. S. DEVELOPMENT OF TREHALASE AND INVERTASE ACTIVITY IN NEUROSPORA. J Bacteriol. 1964 Dec;88:1556–1566. doi: 10.1128/jb.88.6.1556-1566.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hanks D. L., Sussman A. S. Control of trehalase synthesis in Neurospora crassa. Am J Bot. 1969 Nov-Dec;56(10):1160–1166. [PubMed] [Google Scholar]
  10. Hanks D. L., Sussman A. S. The relation between growth, conidiation and trehalase activity in Neurospora crassa. Am J Bot. 1969 Nov-Dec;56(10):1152–1159. [PubMed] [Google Scholar]
  11. Hey A. E., Elbein A. D. Partial prufication and properties of a trehalase from Streptomyces hygroscopicus. J Bacteriol. 1968 Jul;96(1):105–110. doi: 10.1128/jb.96.1.105-110.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ishikawa T., Toh-E A., Uno I., Hasunuma K. Isolation and characterization of nuclease mutants in Neurospora crassa. Genetics. 1969 Sep;63(1):75–92. doi: 10.1093/genetics/63.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Küenzi M. T., Fiechter A. Changes in carbohydrate composition and trehalase-activity during the budding cycle of Saccharomyces cerevisiae. Arch Mikrobiol. 1969;64(4):396–407. doi: 10.1007/BF00417021. [DOI] [PubMed] [Google Scholar]
  14. LASKOWSKI M., MARS P. H., LASKOWSKI M. Comparison of trypsin inhibitor from colostrum with other crystalline trypsin inhibitors. J Biol Chem. 1952 Oct;198(2):745–752. [PubMed] [Google Scholar]
  15. LEDERBERG J. The beta-d-galactosidase of Escherichia coli, strain K-12. J Bacteriol. 1950 Oct;60(4):381–392. doi: 10.1128/jb.60.4.381-392.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  17. Lingappa B. T., Sussman A. S. Endogenous Substrates of Dormant, Activated and Germinating Ascospores of Neurospora Tetrasperma. Plant Physiol. 1959 Jul;34(4):466–472. doi: 10.1104/pp.34.4.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. METZENBERG R. L. A gene affecting the repression of invertase and trehalase in Neurospora. Arch Biochem Biophys. 1962 Mar;96:468–474. doi: 10.1016/0003-9861(62)90322-3. [DOI] [PubMed] [Google Scholar]
  19. Messenguy F., Wiame J. -M. The control of ornithinetranscarbamylase activity by arginase in Saccharomyces cerevisiae. FEBS Lett. 1969 Apr;3(1):47–49. doi: 10.1016/0014-5793(69)80093-1. [DOI] [PubMed] [Google Scholar]
  20. SUSSMAN A. S. A comparison of the properties of two forms of tyrosinase from Neurospora crassa. Arch Biochem Biophys. 1961 Dec;95:407–415. doi: 10.1016/0003-9861(61)90169-2. [DOI] [PubMed] [Google Scholar]
  21. Sussman A. S., Lingappa B. T. Role of Trehalose in Ascospores of Neurospora Tetrasperma. Science. 1959 Nov 13;130(3385):1343–1343. doi: 10.1126/science.130.3385.1343. [DOI] [PubMed] [Google Scholar]
  22. Sussman A. S. The dormancy and germination of fungus spores. Symp Soc Exp Biol. 1969;23:99–121. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES