Four major transcriptional responses in the methionine/threonine biosynthetic pathway of <i>Saccharomyces cerevisiae</i>

Mountain, Harry A.; Byström, Andeŕs S.; Larsen, J. T.; Korch, Christopher

doi:10.1002/yea.320070804

Cited by 103 publications

(86 citation statements)

References 73 publications

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“…3b, nt -172 to -162). Mountain et al (32) found that the mRNA of MET5, another gene believed to be necessary for formation of YSiR, is under general amino acid control. However, no sequence data are available for this gene.…”

Section: Resultsmentioning

confidence: 99%

“…This is not possible for YSiR, which seems to lose all prosthetic groups and associated enzymatic activities if treated with denaturing agents (25). All of the S. cerevisiae mutations unambiguously assigned to the step of sulfite reduction, i.e., meti, metS, met8, met1O, and met2O (30,31,52), have been located to different chromosomes, but so far only genes complementing metS and met8 have been cloned (11,32). The MET5 mRNA has a size of 5.5 kb (32), which suggests that it might encode the 167-kDa subunit of YSiR (25).…”

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confidence: 99%

“…All of the S. cerevisiae mutations unambiguously assigned to the step of sulfite reduction, i.e., meti, metS, met8, met1O, and met2O (30,31,52), have been located to different chromosomes, but so far only genes complementing metS and met8 have been cloned (11,32). The MET5 mRNA has a size of 5.5 kb (32), which suggests that it might encode the 167-kDa subunit of YSiR (25). MET8 was sequenced and found to potentially encode a polypeptide of 274 amino acids, but no knowledge as to its function could be gained from the data (11).…”

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confidence: 99%

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Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

1994

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The yeast assimilatory sulfite reductase is a complex enzyme that is responsible for conversion of sulfite into sulfide. To obtain information on the nature of this enzyme, we In Saccharomyces cerevisiae, sulfate taken up from the surrounding environment is converted into sulfite through three enzymatic steps. Sulfite is further reduced to sulfide, which in turn combines with O-acetyl homoserine to form homocysteine and eventually methionine. A central step in this assimilation pathway is conversion of sulfite into sulfide, a six-electron transfer reaction catalyzed by the yeast assimilatory sulfite reductase (YSiR). YSiR was found to be NADPH dependent (35) and to contain the prosthetic groups flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), an iron-sulfur cluster and a nonflavin chromophore (61) later identified as siroheme (46), a uroporphyrinogen III derivative also found in bacterial sulfite reductases (33,34), and nitrite reductase (21). Some methionine auxotrophs of S. cerevisiae were found to possess a defective sulfite reductase devoid of FAD or of FAD and FMN (62). The mutants devoid only of FAD were later assigned to the metlO complementation group and shown to be affected solely in the sulfite reduction step (30,31). The results of Kobayashi and Yoshimoto (25) suggested that YSiR has an ct212 structure and that the molecular mass of

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

1994

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“…The goal of this research is to define the genetic factors leading to sulfide formation so that genetic strategies can then be used to identify or create commercial strains that will not produce hydrogen sulfide under winemaking conditions. Control of the sulfate reduction pathway is multifaceted and responsive to numerous regulatory inputs (6,8,14,26,29,30). As a consequence, mutational change of a wide array of genes may impact sulfide formation and release.…”

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confidence: 99%

“…As a consequence, mutational change of a wide array of genes may impact sulfide formation and release. Sulfite reductase is responsible for reducing sulfite to sulfide and is regulated by general amino acid control, as well as methionine (26). Other research suggests that cysteine or its derivatives, rather than methionine, is the main end product regulating pathway activity (14,29).…”

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Identification of Genes Affecting Hydrogen Sulfide Formation inSaccharomyces cerevisiae

Linderholm

Findleton

Kumar

et al. 2008

Appl Environ Microbiol

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A screen of the Saccharomyces cerevisiae deletion strain set was performed to identify genes affecting hydrogen sulfide (H 2 S) production. Mutants were screened using two assays: colony color on BiGGY agar, which detects the basal level of sulfite reductase activity, and production of H 2 S in a synthetic juice medium using lead acetate detection of free sulfide in the headspace. A total of 88 mutants produced darker colony colors than the parental strain, and 4 produced colonies significantly lighter in color. There was no correlation between the appearance of a dark colony color on BiGGY agar and H 2 S production in synthetic juice media. Sixteen null mutations were identified as leading to the production of increased levels of H 2 S in synthetic juice using the headspace analysis assay. All 16 mutants also produced H 2 S in actual juices. Five of these genes encode proteins involved in sulfur containing amino acid or precursor biosynthesis and are directly associated with the sulfate assimilation pathway. The remaining genes encode proteins involved in a variety of cellular activities, including cell membrane integrity, cell energy regulation and balance, or other metabolic functions. The levels of hydrogen sulfide production of each of the 16 strains varied in response to nutritional conditions. In most cases, creation of multiple deletions of the 16 mutations in the same strain did not lead to a further increase in H 2 S production, instead often resulting in decreased levels.

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Regulation of sulphate assimilation inSaccharomyces cerevisiae

Ono

Kijima

Ishii

et al. 1996

Yeast

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We examined how the activity of O‐acetylserine and O‐acetylhomoserine sulphydrylase (OAS/OAH) SHLase of Saccharomyces cerevisiae is affected by sulphur source added to the growth medium and genetic background of the strain. In a wild‐type strain, the activity was repressed if methionine, cysteine or glutathione was added to the growth medium. However, in a strain deficient of cystathionine γ‐lyase, cysteine and glutathione were repressive, but methionine was not. In strains deficient of serine O‐acetyltransferase (SATase), OAS/OAH SHLase activity was low regardless of sulphur source and was further lowered by cysteine and glutathione, but not by methionine. From these observations, we concluded that S‐adenosylmethionine should be excluded from being the effector for regulation of OAS/OAH SHLase. Instead, we suspected that S. cerevisiae would have the same regulatory system as Escherichia coli for sulphate assimilation; i.e. cysteine inhibits SATase to lower the cellular concentration of OAS which is required for induction of the sulphate assimilation enzymes including OAS/OAH SHLase. Subsequently, we obtained data supporting this speculation.

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Four major transcriptional responses in the methionine/threonine biosynthetic pathway of Saccharomyces cerevisiae

Cited by 103 publications

References 73 publications

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

Identification of Genes Affecting Hydrogen Sulfide Formation inSaccharomyces cerevisiae

Regulation of sulphate assimilation inSaccharomyces cerevisiae

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