Abstract
During the process of sporulation, a/α diploids degrade about 50% of their vegetative proteins. This degradation is not sporulation specific, for asporogenous diploids of a/a mating type degrade their vegetative proteins in a fashion similar to that of their a/α counterparts. Diploids lacking carboxypeptidase Y activity, prc1/prc1, show about 80% of wild-type levels of protein degradation, but are unimpaired in the production of normal asci. Diploids lacking proteinase B activity, prb1/prb1, show about 50% of wild-type levels of protein degradation. The effect on degradation of the proteinase B deficiency is epistatic to the degradation deficit attributable to the carboxypeptidase Y deficiency. The prb1 homozygotes undergo meiosis and produce spores, but the asci and, possibly, the spores are abnormal. Diploids homozygous for the pleiotropic pep4–3 mutation show only 30% of the wild-type levels of degradation when exposed to a sporulation regimen, and do not undergo meiosis or sporulation. Neither proteinase B nor carboxypeptidase Y is necessary for germination of spores.——Approximately half of the colonies arising from a/a or α/α diploids exposed to the sporulation regiment that express an initially heterozygous drug-resistance marker (can1) appear to arise from mating-type switches followed by meiosis and sporulation.
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- Betz H. Loss of sporulation ability in a yeast mutant with low proteinase A levels. FEBS Lett. 1979 Apr 1;100(1):171–174. doi: 10.1016/0014-5793(79)81157-6. [DOI] [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., 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]
- 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]
- Esposito R. E., Esposito M. S. Genetic recombination and commitment to meiosis in Saccharomyces. Proc Natl Acad Sci U S A. 1974 Aug;71(8):3172–3176. doi: 10.1073/pnas.71.8.3172. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hayashi R., Aibara S., Hata T. A unique carboxypeptidase activity of yeast proteinase C. Biochim Biophys Acta. 1970 Aug 15;212(2):359–361. doi: 10.1016/0005-2744(70)90218-4. [DOI] [PubMed] [Google Scholar]
- Hemmings B. A., Zubenko G. S., Jones E. W. Proteolytic inactivation of the NADP-dependent glutamate dehydrogenase in proteinase-deficient mutants of Saccharomyces cerevisiae. Arch Biochem Biophys. 1980 Jul;202(2):657–660. doi: 10.1016/0003-9861(80)90475-0. [DOI] [PubMed] [Google Scholar]
- Jones E. W. Proteinase mutants of Saccharomyces cerevisiae. Genetics. 1977 Jan;85(1):23–33. doi: 10.1093/genetics/85.1.23. [DOI] [PMC free article] [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]
- López S., Gancedo J. M. Effect of metabolic conditions on protein turnover in yeast. Biochem J. 1979 Mar 15;178(3):769–776. doi: 10.1042/bj1780769. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARQUARDT H. ELEKTRONENOPTISCHE UNTERSUCHUNGEN UEBER DIE ASCOSPORENBILDUNG BEI SACCHAROMYCES CEREVISIAE UNTER CYTOLOGISCHEM UND CYTOGENETISCHEM ASPEKT. Arch Mikrobiol. 1963 Sep 16;46:308–320. [PubMed] [Google Scholar]
- Matern H., Betz H., Holzer H. Compartmentation of inhibitors of proteinases A and B and carboxypeptidase Y in yeast. Biochem Biophys Res Commun. 1974 Oct 8;60(3):1051–1057. doi: 10.1016/0006-291x(74)90419-7. [DOI] [PubMed] [Google Scholar]
- McCusker J. H., Haber J. E. Efficient sporulation of yeast in media buffered near pH6. J Bacteriol. 1977 Oct;132(1):180–185. doi: 10.1128/jb.132.1.180-185.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rogers D. T., Saville D., Bussey H. Saccharomyces cerevisiae killer expression mutant kex2 has altered secretory proteins and glycoproteins. Biochem Biophys Res Commun. 1979 Sep 12;90(1):187–193. doi: 10.1016/0006-291x(79)91607-3. [DOI] [PubMed] [Google Scholar]
- Roth R., Halvorson H. O. Sporulation of yeast harvested during logarithmic growth. J Bacteriol. 1969 May;98(2):831–832. doi: 10.1128/jb.98.2.831-832.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwencke J., Magaña-Schwencke N., Laporte J. Yeast protoplasts from stationary and starved cells: preparation, ultrastructure and vacuolar development. Ann Microbiol (Paris) 1977 Jan;128A(1):3–18. [PubMed] [Google Scholar]
- Wolf D. H., Weiser U. Studies on a carboxypeptidase Y mutant of yeast and evidence for a second carboxypeptidase Activity. Eur J Biochem. 1977 Mar 1;73(2):553–556. doi: 10.1111/j.1432-1033.1977.tb11350.x. [DOI] [PubMed] [Google Scholar]