Abstract
Fifty-nine mutants with reduced ability to cleave the chymotrypsin substrate N-acetyl-DL-phenylalanine β-naphthyl ester have been isolated in S. cerevisiae. All have reduced levels of one or more of the three well-characterized proteinases in yeast. All have reduced levels of proteinase C (carboxy-peptidase Y). These mutations define 16 complementation groups.
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Selected References
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- Betz H., Hinze H., Holzer H. Isolation and properties of two inhibitors of proteinase B from yeast. J Biol Chem. 1974 Jul 25;249(14):4515–4521. [PubMed] [Google Scholar]
- Betz H., Weisner U. Protein degradation and proteinases during yeast sporulation. Eur J Biochem. 1976 Feb 2;62(1):65–76. doi: 10.1111/j.1432-1033.1976.tb10098.x. [DOI] [PubMed] [Google Scholar]
- Cabib E., Farkas V. The control of morphogenesis: an enzymatic mechanism for the initiation of septum formation in yeast. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2052–2056. doi: 10.1073/pnas.68.9.2052. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cabib E., Ulane R., Bowers B. Yeast chitin synthetase. Separation of the zymogen from its activating factor and recovery of the latter in the vacuole fraction. J Biol Chem. 1973 Feb 25;248(4):1451–1458. [PubMed] [Google Scholar]
- Cabib E., Ulane R. Chitin synthetase activating factor from yeast, a protease. Biochem Biophys Res Commun. 1973 Jan 4;50(1):186–191. doi: 10.1016/0006-291x(73)91081-4. [DOI] [PubMed] [Google Scholar]
- Chen A. W., Miller J. J. Proteolytic activity of intact yeast cells during sporulation. Can J Microbiol. 1968 Sep;14(9):957–963. doi: 10.1139/m68-159. [DOI] [PubMed] [Google Scholar]
- Esposito M. S., Esposito R. E., Arnaud M., Halvorson H. O. Acetate utilization and macromolecular synthesis during sporulation of yeast. J Bacteriol. 1969 Oct;100(1):180–186. doi: 10.1128/jb.100.1.180-186.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haas E., Elkana Y., Kulka R. G. A sensitive fluorometric assay for alpha-chymotrypsin. Anal Biochem. 1971 Mar;40(1):218–226. doi: 10.1016/0003-2697(71)90095-9. [DOI] [PubMed] [Google Scholar]
- Hasilik A., Holzer H. Participation of the tryptophan synthase inactivating system from yeast in the activation of chitin synthase. Biochem Biophys Res Commun. 1973 Jul 17;53(2):552–559. doi: 10.1016/0006-291x(73)90697-9. [DOI] [PubMed] [Google Scholar]
- Hopper A. K., Magee P. T., Welch S. K., Friedman M., Hall B. D. Macromolecule synthesis and breakdown in relation to sporulation and meiosis in yeast. J Bacteriol. 1974 Aug;119(2):619–628. doi: 10.1128/jb.119.2.619-628.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Katsunuma T., Schött E., Elsässer S., Holzer H. Purification and properties of tryptophan-synthase-inactivating enzymes from yeast. Eur J Biochem. 1972 Jun 9;27(3):520–526. doi: 10.1111/j.1432-1033.1972.tb01868.x. [DOI] [PubMed] [Google Scholar]
- Lenney J. F., Matile P., Wiemken A., Schellenberg M., Meyer J. Activities and cellular localization of yeast proteases and their inhibitors. Biochem Biophys Res Commun. 1974 Oct 23;60(4):1378–1383. doi: 10.1016/0006-291x(74)90350-7. [DOI] [PubMed] [Google Scholar]