Abstract
A spontaneous, single-gene mutation responsible for a total lack of invertase activity in Neurospora crassa is described. The mutation is believed to lie in the structural gene for invertase, since an immunologically cross-reacting protein is made by the mutant strain. In addition, there was no evidence for a defect in regulation of invertase activity or synthesis by the following criteria. (i) The invertaseless condition was recessive in heterokaryons; (ii) no invertase inhibitor was found in mutant extracts by mixing experiments; and (iii) none of the several sugars able to induce activity in wild-type strains was able to induce activity in the mutant strain. It was also discovered that most of the wild-type enzyme (55 to 75%) cannot be washed free from the rapidly sedimenting cell debris. This finding provided additional support for the hypothesis that Neurospora invertase is located within or about the cell wall.
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- Arnold W. N. Beta-fructofuranosidase from grape berries. II. Solubilization of a bound fraction. Biochim Biophys Acta. 1966 Oct 17;128(1):124–129. doi: 10.1016/0926-6593(66)90148-2. [DOI] [PubMed] [Google Scholar]
- Arnold W. N. Beta-fructofuranosidase from grape berries. Biochim Biophys Acta. 1965 Oct 25;110(1):134–147. doi: 10.1016/s0926-6593(65)80102-3. [DOI] [PubMed] [Google Scholar]
- Atwood K C, Mukai F. Nuclear Distribution in Conidia of Neurospora Heterokaryons. Genetics. 1955 Jul;40(4):438–443. doi: 10.1093/genetics/40.4.438. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HILL E. P., SUSSMAN A. S. PURIFICATION AND PROPERTIES OF TREHALASE (S) FROM NEUROSPORA. Arch Biochem Biophys. 1963 Sep;102:389–396. doi: 10.1016/0003-9861(63)90246-7. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- METZENBERG R. L. ENZYMICALLY ACTIVE SUBUNITS OF NEUROSPORA INVERTASE. Biochim Biophys Acta. 1964 Aug 26;89:291–302. doi: 10.1016/0926-6569(64)90217-2. [DOI] [PubMed] [Google Scholar]
- METZENBERG R. L. THE LOCALIZATION OF BETA-FRUCTOFURANOSIDASE IN NEUROSPORA. Biochim Biophys Acta. 1963 Nov 8;77:455–465. doi: 10.1016/0006-3002(63)90521-3. [DOI] [PubMed] [Google Scholar]
- METZENBERG R. L. The purification and properties of invertase of Neurospora. Arch Biochem Biophys. 1963 Mar;100:503–511. doi: 10.1016/0003-9861(63)90118-8. [DOI] [PubMed] [Google Scholar]
- MYRBACK K. Studies on yeast invertase; soluble and insoluble invertase (saccharase) of baker's yeast. Arch Biochem Biophys. 1957 Jul;69:138–148. doi: 10.1016/0003-9861(57)90481-2. [DOI] [PubMed] [Google Scholar]
- Prout T, Huebschman C, Levene H, Ryan F J. The Proportions of Nuclear Types in Neurospora Heterocaryons as Determined by Plating Conidia. Genetics. 1953 Sep;38(5):518–529. doi: 10.1093/genetics/38.5.518. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sargent M. L., Woodward D. O. Genetic determinants of circadian rhythmicity in Neurospora. J Bacteriol. 1969 Feb;97(2):861–866. doi: 10.1128/jb.97.2.861-866.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suskind S. R., Yanofsky C., Bonner D. M. ALLELIC STRAINS OF Neurospora LACKING TRYPTOPHAN SYNTHETASE: A PRELIMINARY IMMUNOCHEMICAL CHARACTERIZATION. Proc Natl Acad Sci U S A. 1955 Aug 15;41(8):577–582. doi: 10.1073/pnas.41.8.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trevithick J. R., Metzenberg R. L. Molecular sieving by Neurospora cell walls during secretion of invertase isozymes. J Bacteriol. 1966 Oct;92(4):1010–1015. doi: 10.1128/jb.92.4.1010-1015.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vaughan D., Macdonald I. R. Development of soluble and insoluble invertase activity in washed storage tissue slices. Plant Physiol. 1967 Mar;42(3):456–458. doi: 10.1104/pp.42.3.456. [DOI] [PMC free article] [PubMed] [Google Scholar]