Cited by 56Fungal and yeast genetics researchNitrogen and Sulfur Effects on BrassicaMetalloenzymes and iron-sulfur proteins

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

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Hansen, J, Cherest, H, Kielland-Brandt, M C·1994·Journal of Bacteriology

Abstract

The yeast assimilatory sulfate reductase is a complex enzyme that is responsible for conversion of sulfite into sulfide. To obtain information on the nature of this enzyme, we isolated and sequenced the MET10 gene of Saccharomyces cerevisiae and a divergent MET10 allele from Saccharomyces carlsbergensis. The polypeptides deduced from the identically sized open reading frames (1,035 amino acids) of both MET10 genes have molecular masses of around 115 kDa and are 88% identical to each other. The transcript of S. cerevisiae MET10 has a size comparable to that of the open reading frame and is transcriptionally repressed by methionine in a way similar to that seen for other MET genes of S. cerevisiae. Distinct homology was found between the putative MET10-encoded polypeptide and flavin-interacting parts of the sulfite reductase flavoprotein subunit (encoded by cysJ) from Escherichia coli and several other flavoproteins. A significant N-terminal homology to pyruvate flavodoxin oxidoreductase (encoded by nifJ) from Klebsiella pneumoniae, together with a lack of obvious flavin mononucleotide-binding motifs in the MET10 deduced amino acid sequence, suggests that the yeast assimilatory sulfite reductase is a distinct type of sulfite reductase.

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Crossref · 10.1128/jb.176.19.6050-6058.1994

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  • Sulfite reductase is a heterotetramer of two α and two β subunits encoded by MET10 and MET5.

    “Sulfite reductase is a heterotetramer, consisting of two αand two β-subunits, which are encoded by MET10 and MET5 genes, respectively (Kobayashi and Yoshimoto 1982, Hansen et al. 1994, Sutherland et al. 2003).”

    From Yeast and bacterial modulation of wine aroma and flavour (2005) · cites this paper as Hansen et al. 1994

    The introduction reports that earlier results suggested an α2β2 structure, and the paper identifies MET10 as encoding the α subunit. It says the size of MET5 mRNA suggests MET5 might encode the β subunit; it does not establish that assignment or the subunit arrangement as fact. (LLM, conf=0.87)

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Research works printed but not linked: 7

  1. [1]1. Arndt, K., and G. R. Fink. 1986. GCN4 protein, a positive transcription factor in yeast, binds general control promoters at all 5' TGACTC 3' sequences. Proc. Natl. Acad. Sci. USA 83:8516– 8520.
  2. [13]13. Gjermansen, C. 1991. Comparison of genes in Saccharomyces cerevisiae and Saccharomyces carlsbergensis. Ph.D. thesis. University of Copenhagen, Copenhagen, Denmark.
  3. [16]16. Hadfield, C. 1994. Construction of cloning and expression vectors, p. 17–48. In J. R. Johnston (ed.), Molecular genetics of yeast. A practical approach. Oxford University Press, Öxford.
  4. [24]24. Kielland-Brandt, M. C., T. Nilsson-Tillgren, C. Gjermansen, S. Holmberg, and M. B. Pedersen. Genetics of brewing yeast. In A. H. Rose, J. S. Harrison, and A. E. Wheals (ed.), The yeasts, 2nd ed., vol. 6, in press. Academic Press, London.
  5. [42]42. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
  6. [44]44. Scherer, S., and R. W. Davis. 1979. Replacement of chromosome segments with altered DNA sequences constructed in vitro. Proc. Natl. Acad. Sci. USA 76:4951–4955.
  7. [58]58. Watenpaugh, K. D., L. C. Sieker, and L. H. Jensen. 1973. The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0 Å resolution. Proc. Natl. Acad. Sci. USA 70:3857–3860.

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Authors
Hansen, J., Cherest, H., & Kielland-Brandt, M. C.
Affiliations
  • Carlsberg Laboratory (DK)
  • Department of Yeast Genetics, Carlsberg Laboratory, Copenhagen Valby, Denmark.
Venue
Journal of Bacteriology
Published
1994-10
Volume
176
Issue
19
Pages
6050-6058
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W1943939928
Cited by
56
References
0
Citations by year
2026: 1 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 4 · 2016: 1 · 2014: 2 · 2013: 1 · 2012: 2
FWCI
1.27
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nitrogen and Sulfur Effects on Brassica
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
Saccharomyces cerevisiae, Saccharomyces carlsbergensis, alpha subunit, FAD binding site, NADPH binding site, methionine repression, flavoprotein, sulfate assimilation
MeSH terms
Amino Acid Sequence, Base Sequence, Cloning, Molecular, Enzyme Repression, Flavin-Adenine Dinucleotide, Flavoproteins, Genes, Fungal, Methionine, Molecular Sequence Data, NADP, Oxidation-Reduction, Protein Conformation, RNA, Messenger, Saccharomyces, Saccharomyces cerevisiae, Sulfites, Gene Expression Regulation, Fungal, Sequence Homology, Amino Acid, Sequence Analysis, DNA, Oxidoreductases Acting on Sulfur Group Donors, Sulfite Reductase (NADPH)

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