Abstract
This report describes the isolation of the genes encoding allantoicase (DAL2) and ureidoglycolate hydrolase (DAL3), which are components of the large DAL gene cluster on the right arm of chromosome IX of Saccharomyces cerevisiae. During this work a new gene (DAL7) was identified and found to be regulated in the manner expected for an allantoin pathway gene. Its expression was (i) induced by allophanate, (ii) sensitive to nitrogen catabolite repression, and (iii) responsive to mutation of the DAL80 and DAL81 loci, which have previously been shown to regulate the allantoin degradation system. Hybridization probes generated from these cloned genes were used to analyze expression of the allantoin pathway genes in wild-type and mutant cells grown under a variety of physiological conditions. When comparison was possible, the patterns of mRNA and enzyme levels observed in various strains and physiological conditions were very similar, suggesting that the system is predominantly regulated at the level of gene expression. Although all of the genes seem to be controlled by a common mechanism, their detailed patterns of expression were, at the same time, highly individual and diverse.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bossinger J., Cooper T. G. Execution times of macromolecular synthetic processes involved in the induction of allophanate hydrolase at 15 degrees C. J Bacteriol. 1976 Oct;128(1):498–501. doi: 10.1128/jb.128.1.498-501.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Buckholz R. G., Cooper T. G. Oxalurate induction of multiple URA3 transcripts in Saccharomyces cerevisiae. Mol Cell Biol. 1983 Nov;3(11):1889–1897. doi: 10.1128/mcb.3.11.1889. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carlson M., Botstein D. Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase. Cell. 1982 Jan;28(1):145–154. doi: 10.1016/0092-8674(82)90384-1. [DOI] [PubMed] [Google Scholar]
- Chisholm G., Cooper T. G. Isolation and characterization of mutants that produce the allantoin-degrading enzymes constitutively in Saccharomyces cerevisiae. Mol Cell Biol. 1982 Sep;2(9):1088–1095. doi: 10.1128/mcb.2.9.1088. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Choi K. S., Lee K. W., Roush A. H. The assay of yeast ureidoglycolatase. Anal Biochem. 1966 Dec;17(3):413–422. doi: 10.1016/0003-2697(66)90177-1. [DOI] [PubMed] [Google Scholar]
- Clarke L., Carbon J. Functional expression of cloned yeast DNA in Escherichia coli: specific complementation of argininosuccinate lyase (argH) mutations. J Mol Biol. 1978 Apr 25;120(4):517–532. doi: 10.1016/0022-2836(78)90351-0. [DOI] [PubMed] [Google Scholar]
- Cooper T. G., Lawther R. P. Induction of the allantoin degradative enzymes in Saccharomyces cerevisiae by the last intermediate of the pathway. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2340–2344. doi: 10.1073/pnas.70.8.2340. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fyrberg E. A., Kindle K. L., Davidson N., Kindle K. L. The actin genes of Drosophila: a dispersed multigene family. Cell. 1980 Feb;19(2):365–378. doi: 10.1016/0092-8674(80)90511-5. [DOI] [PubMed] [Google Scholar]
- LEE K. W., ROUSH A. H. ALLANTOINASE ASSAYS AND THEIR APPLICATION TO YEAST AND SOYBEAN ALLANTOINASES. Arch Biochem Biophys. 1964 Dec;108:460–467. doi: 10.1016/0003-9861(64)90427-8. [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]
- Lawther R. P., Cooper T. G. Kinetics of induced and repressed enzyme synthesis in Saccharomyces cerevisiae. J Bacteriol. 1975 Mar;121(3):1064–1073. doi: 10.1128/jb.121.3.1064-1073.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lemoine Y., Dubois E., Wiame J. M. The regulation of urea amidolyase of Saccharomyces cerevisiae: mating type influence on a constitutivity mutation acting in cis. Mol Gen Genet. 1978 Nov 9;166(3):251–258. [PubMed] [Google Scholar]
- Nasmyth K. A., Reed S. I. Isolation of genes by complementation in yeast: molecular cloning of a cell-cycle gene. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2119–2123. doi: 10.1073/pnas.77.4.2119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Orr-Weaver T. L., Szostak J. W., Rothstein R. J. Yeast transformation: a model system for the study of recombination. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6354–6358. doi: 10.1073/pnas.78.10.6354. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perkins D. D. Biochemical Mutants in the Smut Fungus Ustilago Maydis. Genetics. 1949 Sep;34(5):607–626. doi: 10.1093/genetics/34.5.607. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rothstein R. J. One-step gene disruption in yeast. Methods Enzymol. 1983;101:202–211. doi: 10.1016/0076-6879(83)01015-0. [DOI] [PubMed] [Google Scholar]
- Struhl K., Stinchcomb D. T., Scherer S., Davis R. W. High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1035–1039. doi: 10.1073/pnas.76.3.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sumrada R. A., Cooper T. G. Isolation of the CAR1 gene from Saccharomyces cerevisiae and analysis of its expression. Mol Cell Biol. 1982 Dec;2(12):1514–1523. doi: 10.1128/mcb.2.12.1514. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sumrada R., Cooper T. G. Oxaluric acid: a non-metabolizable inducer of the allantoin degradative enzymes in Saccharomyces cerevisiae. J Bacteriol. 1974 Mar;117(3):1240–1247. doi: 10.1128/jb.117.3.1240-1247.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Turoscy V., Cooper T. G. Pleiotropic control of five eucaryotic genes by multiple regulatory elements. J Bacteriol. 1982 Sep;151(3):1237–1246. doi: 10.1128/jb.151.3.1237-1246.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winston F., Chumley F., Fink G. R. Eviction and transplacement of mutant genes in yeast. Methods Enzymol. 1983;101:211–228. doi: 10.1016/0076-6879(83)01016-2. [DOI] [PubMed] [Google Scholar]