Cloning, nucleotide sequence, and regulation of MET14, the gene encoding the APS kinase of Saccharomyces cerevisiae

Korch, Christopher; Mountain, Harry A.; Byström, Andeŕs S.

doi:10.1007/bf00264218

Cited by 62 publications

(48 citation statements)

References 74 publications

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“…This result is similar to those for MET2 (3,29), MET3 (10) (43), and SAM] (56). Two identical sequence elements strongly resembling the UASMET consensus sequence TCACGTGA (28,54), which closely matches the RTCAC RTG CDE1 consensus sequence (19), are found in S. cerevisiae MET10 as CACGTGA (Fig. 3a, nt -232 to -226 and nt -250 to -244).…”

Section: Resultsmentioning

confidence: 62%

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: 62%

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 deletion of this element apparently increased the level of MET25 transcription after the cells were grown in the presence of a repressive amount of methionine (22,30). To determine whether this element may constitute a real regulatory component, we wanted to isolate DNA binding factors capable of recognizing this short sequence.…”

Section: Sulfur Amino Acid Metabolism Inmentioning

confidence: 99%

Met31p and Met32p, Two Related Zinc Finger Proteins, Are Involved in Transcriptional Regulation of Yeast Sulfur Amino Acid Metabolism

Blaiseau

Isnard

Surdin-Kerjan

et al. 1997

Molecular and Cellular Biology

113

117

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Sulfur amino acid metabolism inIn the yeast Saccharomyces cerevisiae, the sulfur amino acid biosynthesis pathway is composed of more than 20 unlinked genes whose expression is coordinately regulated: the transcription of the genes is turned off in response to an increase in the intracellular concentration of S-adenosylmethionine (AdoMet), the end product of this pathway (30). Owing to the numerous genetic and biochemical data accumulated so far, this metabolic pathway constitutes a model system for studying the molecular mechanisms allowing specific regulation of gene expression in eucaryotic cells.Previous results have shown that, to a large extent, transcriptional activation of the structural genes from the sulfur network is achieved through the assembly of a multisubunit protein complex which binds to the TCACGTG core sequence, a motif found in the 5Ј upstream region of these genes (24). This complex associates two basic leucine zipper factors, Met4p and Met28p, with a basic helix-loop-helix factor, Cbf1p. Recent in vitro reconstitution experiments have confirmed that the Cbf1p-Met4p-Met28p complex can form without additional factors on the TCACGTG sequence present upstream of the MET16 gene (23). Functional analysis of each subunit has demonstrated that the Cbf1p-Met4p-Met28p complex contains only one transcription activation module, which is provided by the Met4p subunit. Met4p was indeed shown to contain a unique activation domain located in the N-terminal part of the protein and whose function is controlled by the level of intracellular AdoMet (25). In contrast, the Cbf1p and Met28p subunit functions were shown to be dedicated to DNA recognition and complex formation (23). Moreover, the Cbf1p-Met4p-Met28p complex exhibits another interesting feature, being composed of two sulfur-specific factors, Met4p and Met28p, and one multifunctional factor, Cbf1p, which is involved in both regulation of sulfur amino acid metabolism and chromosome stability (2, 7, 31). Indeed, Cbf1p binds to the CDE1 sequence, one of the three DNA elements which constitute the centromeres of Saccharomyces cerevisiae chromosomes (1, 16).In addition to the three components of the Cbf1p-Met4p-Met28p complex, the AdoMet-mediated regulation of the sulfur network involves the Met30 protein, a member of the WD40 protein family (32). Met30p was shown to function by inhibiting the transcription activation function of Met4p when the level of intracellular AdoMet is high. Furthermore, as expected from the results of the functional analyses of Met4p, Met30p was shown to interact in vivo with Met4p, with this interaction requiring the Met4p inhibitory region (32).Although the Cbf1p-Met4p-Met28p and Met30p family seems to constitute the main molecular determinant allowing the specific regulation of the sulfur network, mutational analysis of the MET25 5Ј upstream region had identified another cis-acting element. The deletion of this element apparently increased the level of MET25 transcription after the cells were grown in the presence of a repressi...

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“…Sulphate reduction requires first an initial 'activation' to phosphosulphate compounds. As in Escherichia coli and Salmonella typhimurium, this activation is a two-step process in S. cerevisiae : ATP sulphurylase (encoded by the MET3 gene; Cherest et al, 1987) first catalyses the reaction of ATP and sulphate to give adenosine 5'-phosphosulphate (APS); then APS kinase (encoded by the MET14 gene, Korch et al, 1991) carries out a phosphorylation step that leads to the formation of 3'-phosphoadenosine 5'-phosphosulphate (PAPS). The reduction of the sulphur atom is then achieved through two enzymic reactions.…”

Section: Introductionmentioning

confidence: 99%

Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation

Thomas

Barbey

Henry

et al. 1992

Journal of General Microbiology

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The assimilation of sulphate in Saccharomyces cereuisiae, comprising the reduction of sulphate to sulphide and the incorporation of the sulphur atom into a four-carbon chain, requires the integrity of 13 different genes. To date, the functions of nine of these genes are still not clearly established. A set of strains, each bearing a mutation in one MET gene, was studied. Phenotypic studies and enzyme determinations showed that the products of at least five genes are needed for the synthesis of an enzymically active sulphite reductase. These genes are METl, METS, MET4 MET10 and MET20. Wild-type strains of S. cereuisiae can use organic metabolites such as homocysteine, cysteine, methionine and S-adenosylmethionine as sulphur sources. They are also able to use inorganic sulphur sources such as sulphate, sulphite, sulphide or thiosulphate. Here we show that both of the two sulphur atoms of thiosulphate are used by S. cereuisiae. Thiosulphate is cleaved into sulphite and sulphide prior to utilization by the sulphate assimilation pathway, as the metabolism of one sulphur atom from thiosulphate requires the presence of an active sulphite reductase.

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Cloning, nucleotide sequence, and regulation of MET14, the gene encoding the APS kinase of Saccharomyces cerevisiae

Cited by 62 publications

References 74 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

Met31p and Met32p, Two Related Zinc Finger Proteins, Are Involved in Transcriptional Regulation of Yeast Sulfur Amino Acid Metabolism

Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation

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