Abstract
We have identified a mutation in a gene of Saccharmyces cerevisiae, STR1, that leads to a strict nutritional requirement for cysteine. The str1-1 mutation decreases to an undetectable level the cystathionine γ-lyase activity. This enzyme catalyzes one of the two reactions involved in the transsulfuration pathway that yields cysteine from homocysteine with the intermediary formation of cystathionine. The phenotype induced by this mutation implies that, in S. cerevisiae, the sulfur atom of sulfide resulting from the reductive assimilation of sulfate is incorporated into a four carbon backbone yielding homocysteine, which, in turn, is the precursor of the biosynthesis of both cysteine and methionine. This also reveals that the direct synthesis of cysteine by incorporation of the sulfur atom into a three carbon backbone as found in Escherichia coli does not occur in S. cerevisiae. The study of the meiotic progeny of diploid strains heterozygous at the STR1 locus has shown that the str1-1 mutation undergoes a particularly high frequency of meiotic gene conversion.
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- Beatty P. W., Reed D. J. Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes. Arch Biochem Biophys. 1980 Oct 1;204(1):80–87. doi: 10.1016/0003-9861(80)90009-0. [DOI] [PubMed] [Google Scholar]
- Belfaiza J., Parsot C., Martel A., de la Tour C. B., Margarita D., Cohen G. N., Saint-Girons I. Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc Natl Acad Sci U S A. 1986 Feb;83(4):867–871. doi: 10.1073/pnas.83.4.867. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burnett G., Marcotte P., Walsh C. Mechanism-based inactivation of pig heart L-alanine transaminase by L-propargylglycine. Half-site reactivity. J Biol Chem. 1980 Apr 25;255(8):3487–3491. [PubMed] [Google Scholar]
- Byrne C. R., Monroe R. S., Ward K. A., Kredich N. M. DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH. J Bacteriol. 1988 Jul;170(7):3150–3157. doi: 10.1128/jb.170.7.3150-3157.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cherest H., Eichler F., Robichon-Szulmajster H. Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae. J Bacteriol. 1969 Jan;97(1):328–336. doi: 10.1128/jb.97.1.328-336.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gaitonde M. K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J. 1967 Aug;104(2):627–633. doi: 10.1042/bj1040627. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kashiwamata S., Greenberg D. M. Studies on cystathionine synthase of rat liver. Properties of the highly purified enzyme. Biochim Biophys Acta. 1970 Sep 16;212(3):488–500. doi: 10.1016/0005-2744(70)90255-x. [DOI] [PubMed] [Google Scholar]
- Kerjan P., Cherest H., Surdin-Kerjan Y. Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene. Nucleic Acids Res. 1986 Oct 24;14(20):7861–7871. doi: 10.1093/nar/14.20.7861. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kredich N. M., Tomkins G. M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J Biol Chem. 1966 Nov 10;241(21):4955–4965. [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]
- Masselot M., De Robichon-Szulmajster H. Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants. Mol Gen Genet. 1975 Aug 5;139(2):121–132. doi: 10.1007/BF00264692. [DOI] [PubMed] [Google Scholar]
- Ono B., Shirahige Y., Nanjoh A., Andou N., Ohue H., Ishino-Arao Y. Cysteine biosynthesis in Saccharomyces cerevisiae: mutation that confers cystathionine beta-synthase deficiency. J Bacteriol. 1988 Dec;170(12):5883–5889. doi: 10.1128/jb.170.12.5883-5889.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ono B., Suruga T., Yamamoto M., Yamamoto S., Murata K., Kimura A., Shinoda S., Ohmori S. Cystathionine accumulation in Saccharomyces cerevisiae. J Bacteriol. 1984 Jun;158(3):860–865. doi: 10.1128/jb.158.3.860-865.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Paszewski A., Grabski J. Regulation of S-amino acids biosynthesis in Aspergillus nidulans. Role of cysteine and-or homocysteine as regulatory effectors. Mol Gen Genet. 1974;132(4):307–320. doi: 10.1007/BF00268571. [DOI] [PubMed] [Google Scholar]
- Pieniazek N. J., Bal J., Balbin E., Stepién P. P. An Aspergillus nidulans mutant lacking serine transacetylase: evidence for two pathways of cysteine biosynthesis. Mol Gen Genet. 1974;132(4):363–366. doi: 10.1007/BF00268575. [DOI] [PubMed] [Google Scholar]
- Pieniazek N. J., Bal J., Balbin E., Stepién P. P. An Aspergillus nidulans mutant lacking serine transacetylase: evidence for two pathways of cysteine biosynthesis. Mol Gen Genet. 1974;132(4):363–366. doi: 10.1007/BF00268575. [DOI] [PubMed] [Google Scholar]
- Piotrowska M., Kruszewska A., Paszewski A. Effect of regulatory mutations of sulphur metabolism on the levels of cysteine- and homocysteine-synthesizing enzymes in Neurospora crassa. Acta Biochim Pol. 1980;27(3-4):395–403. [PubMed] [Google Scholar]
- Sangsoda S., Cherest H., Surdin-Kerjan Y. The expression of the MET25 gene of Saccharomyces cerevisiae is regulated transcriptionally. Mol Gen Genet. 1985;200(3):407–414. doi: 10.1007/BF00425724. [DOI] [PubMed] [Google Scholar]
- Sirko A., Hryniewicz M., Hulanicka D., Böck A. Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide sequence and expression of the cysTWAM gene cluster. J Bacteriol. 1990 Jun;172(6):3351–3357. doi: 10.1128/jb.172.6.3351-3357.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tanase S., Morino Y. Irreversible inactivation of aspartate aminotransferases during transamination with L-propargylglycine. Biochem Biophys Res Commun. 1976 Feb 23;68(4):1301–1308. doi: 10.1016/0006-291x(76)90338-7. [DOI] [PubMed] [Google Scholar]
- Thomas D., Cherest H., Surdin-Kerjan Y. Elements involved in S-adenosylmethionine-mediated regulation of the Saccharomyces cerevisiae MET25 gene. Mol Cell Biol. 1989 Aug;9(8):3292–3298. doi: 10.1128/mcb.9.8.3292. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamagata S. Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae. J Bacteriol. 1987 Aug;169(8):3458–3463. doi: 10.1128/jb.169.8.3458-3463.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamagata S. Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms. Biochimie. 1989 Nov-Dec;71(11-12):1125–1143. doi: 10.1016/0300-9084(89)90016-3. [DOI] [PubMed] [Google Scholar]
- Yamagata S., Takeshima K., Naiki N. Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast. J Biochem. 1974 Jun;75(6):1221–1229. doi: 10.1093/oxfordjournals.jbchem.a130505. [DOI] [PubMed] [Google Scholar]
- Yamagata S., Takeshima K., Naiki N. O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast; studies with methionine auxotrophs. J Biochem. 1975 May;77(5):1029–1036. doi: 10.1093/oxfordjournals.jbchem.a130803. [DOI] [PubMed] [Google Scholar]
