Metabolism of sulfur amino acids in Saccharomyces cerevisiae.

Thomas, Dominique; Surdin-Kerjan, Y

doi:10.1128/.61.4.503-532.1997

Cited by 518 publications

(338 citation statements)

References 221 publications

(347 reference statements)

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“…In all the following repression experiments, the negative regulation of the MET gene network was triggered by growing the cells in the presence of 1 mM L-methionine. As already demonstrated, repression of the MET genes actually results from the rapid conversion of methionine into AdoMet (Thomas et al, 1988;Thomas and Surdin-Kerjan, 1997). Repression kinetics of five MET genes, each specific for one step of the sulfate assimilation pathway, were monitored by Northern analysis in cdc34-2, cdc53-1, met30-2 and skp1-11 SCF mutant strains.…”

Section: Scf Met30 Controls the Overall Sulfate Assimilation Pathwaymentioning

confidence: 87%

Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCFMet30 complex

Rouillon

Barbey

Patton

et al. 2000

EMBO J

156

159

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Saccharomyces cerevisiae SCF Met30 ubiquitin-protein ligase controls cell cycle function and sulfur amino acid metabolism. We report here that the SCF Met30 complex mediates the transcriptional repression of the MET gene network by triggering degradation of the transcriptional activator Met4p when intracellular S-adenosylmethionine (AdoMet) increases. This AdoMet-induced Met4p degradation is dependent upon the 26S proteasome function. Unlike Met4p, the other components of the specific transcriptional activation complexes that are assembled upstream of the MET genes do not appear to be regulated at the protein level. We provide evidence that the interaction between Met4p and the F-box protein Met30p occurs irrespective of the level of intracellular AdoMet, suggesting that the timing of Met4p degradation is not controlled by its interaction with the SCF Met30 complex. We also demonstrate that Met30p is a short-lived protein, which localizes within the nucleus. Furthermore, transcription of the MET30 gene is regulated by intracellular AdoMet levels and is dependent upon the Met4p transcription activation function. Thus Met4p appears to control its own degradation by regulating the amount of assembled SCF Met30 ubiquitin ligase.

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Section: Scf Met30 Controls the Overall Sulfate Assimilation Pathwaymentioning

confidence: 87%

Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCFMet30 complex

Rouillon

Barbey

Patton

et al. 2000

EMBO J

156

159

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“…The CYS3 protein is also subject to rapid turnover in response to changes in sulfur supply [302]. Related control mechanisms are also present in the yeast S. cerevisiae [9,303]. In the cyanobacterium Synechococcus sp.…”

Section: Regulation Of Bacterial Organosulfur Metabolismmentioning

confidence: 99%

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

2000

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Sulfonates and sulfate esters are widespread in nature, and make up over 95% of the sulfur content of most aerobic soils. Many microorganisms can use sulfonates and sulfate esters as a source of sulfur for growth, even when they are unable to metabolize the carbon skeleton of the compounds. In these organisms, expression of sulfatases and sulfonatases is repressed in the presence of sulfate, in a process mediated by the LysR-type regulator protein CysB, and the corresponding genes therefore constitute an extension of the cys regulon. Additional regulator proteins required for sulfonate desulfonation have been identified in Escherichia coli (the Cbl protein) and Pseudomonas putida (the AsfR protein). Desulfonation of aromatic and aliphatic sulfonates as sulfur sources by aerobic bacteria is oxygendependent, carried out by the K-ketoglutarate-dependent taurine dioxygenase, or by one of several FMNH 2 -dependent monooxygenases. Desulfurization of condensed thiophenes is also FMNH 2 -dependent, both in the rhodococci and in two Gram-negative species. Bacterial utilization of aromatic sulfate esters is catalyzed by arylsulfatases, most of which are related to human lysosomal sulfatases and contain an active-site formylglycine group that is generated post-translationally. Sulfate-regulated alkylsulfatases, by contrast, are less well characterized. Our increasing knowledge of the sulfur-regulated metabolism of organosulfur compounds suggests applications in practical fields such as biodesulfurization, bioremediation, and optimization of crop sulfur nutrition. ß

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“…Therefore, we recently found that a large amount of L-cysteine was produced in E. coli strains when expressing the gene encoding feedback inhibitioninsensitive SATase [13,19,20]. Regulation of S. cerevisiae sulfur metabolism is still controversial with regard to whether S-adenosylmethionine acts as a co-repressor in strains de¢cient in SATase activity [21,22] or OAS acts as a co-inducer in strains having SATase activity [5,15]. Thus, identi¢cation of the transcriptional regulator in S. cerevisiae, corresponding to MetJ protein, the E. coli met repressor [23,24], or the E. coli CysB protein, is worthy of further study.…”

Section: Strain or Plasmidmentioning

confidence: 99%

Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis

Takagi

2003

FEMS Microbiology Letters

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Some strains of Saccharomyces cerevisiae have detectable activities of L-serine O-acetyltransferase (SATase) and O-acetyl-L-serine/O-acetyl-L-homoserine sulfhydrylase (OAS/OAH-SHLase), but synthesize L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. To untangle this peculiar feature in sulfur metabolism, we introduced Escherichia coli genes encoding SATase and OAS-SHLase into S. cerevisiae L-cysteine auxotrophs. While the cells expressing SATase grew on medium lacking L-cysteine, those expressing OAS-SHLase did not grow at all. The cells expressing both enzymes grew very well without L-cysteine. These results indicate that S. cerevisiae SATase cannot support L-cysteine biosynthesis and that S. cerevisiae OAS/OAH-SHLase produces L-cysteine if enough OAS is provided by E. coli SATase. It appears as if S. cerevisiae SATase does not possess a metabolic role in vivo either because of very low activity or localization. For example, S. cerevisiae SATase may be localized in the nucleus, thus controlling the level of OAS required for regulation of sulfate assimilation, but playing no role in the direct synthesis of L-cysteine.

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Metabolism of sulfur amino acids in Saccharomyces cerevisiae.

Cited by 518 publications

References 221 publications

Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCFMet30 complex

Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCFMet30 complex

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis

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