Reference |
| PMID | Title & Author | Abstract | Year |
0 | 2989110 | Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae.H Cherest, N T Nguyen, Y Surdin-Kerjan | The MET3 gene, coding for ATP sulfurylase (ATPS), an enzyme implicated in methionine biosynthesis in Saccharomyces cerevisiae, was cloned by functional complementation, after transformation, of a yeast met3 mutant strain. The cloned MET3 gene was used as a probe to measure the specific MET3 messenger RNA in a wild-type strain grown under conditions which promote or fail to promote repression of ATPS synthesis. It was found that the level of MET3 messenger RNA is reduced ten-fold when the strain is grown under conditions where ATPS synthesis is repressed, suggesting that the MET3 expression is regulated transcriptionally. The direction of transcription and the size of the transcript have been determined. | 1985 |
1 | 12177356 | Molecular and genetic analysis of the Cryptococcus neoformans MET3 gene and a met3 mutant.Zhonghui Yang , Renata C Pascon , Andrew Alspaugh , Gary M Cox , John H McCusker | The Cryptococcus neoformans MET3 cDNA (encoding ATP sulfurylase) was cloned by complementation of the corresponding met3 mutation in Saccharomyces cerevisiae. Sequence analysis showed high similarity between the deduced amino acid sequence of the C. neoformans Met3p and other fungal ATP sulfurylases. A C. neoformans met3 mutant was made by targeted insertional mutagenesis, which had the expected auxotrophic phenotype, and reconstituted the met3 mutant to Met(+). In vitro, the C. neoformans met3 mutant had a substantial defect in melanin formation, significantly reduced growth rate, and greatly increased thermotolerance. In the murine inhalation infection model, the met3 mutant was avirulent and was deficient in its ability to survive in mice. It is concluded that, in contrast to the yeast form of Histoplasma capsulatum, in C. neoformans the sulfate-assimilation arm of the methionine biosynthetic pathway plays an important role in vitro, even in the presence of abundant exogenous methionine, and is critical for virulence, and indeed for survival, in vivo. | 2002 |
2 | 3325778 | The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and relationship of the 5' non-coding region to that of MET25.H Cherest , P Kerjan, Y Surdin-Kerjan | In Saccharomyces cerevisiae, the expression of several genes implicated in methionine biosynthesis is co-regulated by a specific negative control. To elucidate the molecular basis of this regulation, we have cloned two of these genes, MET3 and MET25. The sequence of MET25 has already been determined (Kerjan et al. 1986). Here, we report the nucleotide sequence of the MET3 gene along with its 5' and 3' flanking regions. Plasmids bearing different deletions upstream of the transcribed region of MET3 were constructed. They were introduced into yeast cells and tested for their ability to complement met3 mutations and to respond to regulation by exogenous methionine. The regulatory region was located within a 100 bp region. The sequence of this regulatory region was compared with that of MET25. A short common sequence which occurs 250-280 bp upstream of the translation initiation codon of the gene was found. This sequence is a good candidate for the cis-acting regulatory element. | 1987 |
3 | 10092498 | Production, purification, and luminometric analysis of recombinant Saccharomyces cerevisiae MET3 adenosine triphosphate sulfurylase expressed in Escherichia coli.S Karamohamed , J Nilsson, K Nourizad, M Ronaghi, B Pettersson, P Nyrén | ATP sulfurylase cDNA from MET3 on chromosome X of Saccharomyces cerevisiae was amplified and cloned, and recombinant ATP sulfurylase was expressed in Escherichia coli. The synthesis of ATP sulfurylase was directed by an expression system that employs the regulatory genes of the luminous bacterium Vibrio fischeri. A soluble, biologically active form was purified to electrophoretic homogeneity from lysates of recombinant E. coli by ammonium sulfate fractionation, ion-exchange chromatography, and gel filtration. The specific activity of the purified enzyme was estimated to 140 U/mg. The apparent molecular mass of the recombinant enzyme was determined by gel filtration to be 470 kDa, which indicates that the active enzyme is an octamer of identical subunits (the molecular mass of a single subunit is 59.3 kDa). The ATP sulfurylase activity was monitored in real time by a very sensitive bioluminometric method. | 1999 |
4 | 20890097 | The wine yeast strain-dependent expression of genes implicated in sulfide production in response to nitrogen availability.Ana Mendes-Ferreira , Catarina Barbosa, Elena Jimenez-Marti, Marcel Li Del Olmo, Arlete Mendes-Faia | Sulfur metabolism in S. cerevisiae is well established, but the mechanisms underlying the formation of sulfide remain obscure. Here we investigated by real time RT-PCR the dependence of expression levels of MET3, MET5/ECM17, MET10, MET16 and MET17 along with SSU1 on nitrogen availability in two wine yeast strains that produce divergent sulfide profiles. MET3 was the most highly expressed of the genes studied in strain PYCC4072, and SSU1 in strain UCD522. Strains behaved differently according to the sampling times, with UCD522 and PYCC4072 showing the highest expression levels at 120h and 72h, respectively. In the presence of 267mg assimilable N/l, the genes were more highly expressed in strain UCD522 than in PYCC4072. MET5/ECM17 and MET17 were only weakly expressed in both strains under any condition tested. MET10 and SSU1 in both strains, but MET16 only in PYCC4072, were consistently up-regulated when sulfide production was inhibited. This study illustrates that strain genotype could be important in determining enzyme activities and therefore the rate of sulfide liberation. This linkage, for some yeast strains, of sulfide production to expression levels of genes associated to sulfate assimilation and sulfur amino acid biosynthesis could be relevant for defining new strategies for genetic improvement of wine yeasts. | 2010 |
Christensen G A , Zane G M , Kazakov A E , et al. Rex (Encoded by DVU_0916) in Desulfovibrio vulgaris Hildenborough Is a Repressor of Sulfate Adenylyl Transferase and Is Regulated by NADH[J]. Journal of Bacteriology, 2015, 197(1):29-39.
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