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Gene Review

MET16  -  phosphoadenylyl-sulfate reductase...

Saccharomyces cerevisiae S288c

Synonyms: 3'-phosphoadenylylsulfate reductase, P9325.8, PAPS reductase, thioredoxin dependent, PAdoPS reductase, Phosphoadenosine phosphosulfate reductase, ...
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Disease relevance of MET16

  • In the present study, we show that MET16 is the structural gene for PAPS reductase and that the yeast and the Escherichia coli enzymes display significant similarities [1].

High impact information on MET16

  • Here, we demonstrate two phases of combinatorial and dynamic H3 methylation during induction of transcription at MET16 in yeast [2].
  • Thanks to CY306, we also show that TRXs interact with the phosphoadenosine-5-phosphosulfate (PAPS) reductase MET16 through a conserved cysteine [3].
  • A functional comparison of the centromere binding proteins with transcription factors binding at MET16 promoters reveals the strong analogy between centromeres and the MET16 promoter [4].
  • MET16-CYC1-lacZ reporter constructs were used to show that MET16 5'-flanking DNA contains a CP1-dependent upstream activation sequence (UAS) [5].
  • In most respects, MET16-CYC1-lacZ reporter gene expression mirrored that of chromosomal MET16; however, the endogenous gene was found to be activated in response to amino acid starvation (general control) [5].

Chemical compound and disease context of MET16


Biological context of MET16

  • We therefore conclude that the GCN4 dependence of MET16 expression is responsible for the decrease in 5' to 3' digestion under stress conditions and that cells use pAp as a signal to limit 5' to 3' RNA degradation under stress conditions [7].
  • Two strains with low sulphite production were transformed with high-copy plasmids containing either or both MET14 and MET16 [8].
  • Cbf1p is a sequence specific DNA binding protein required for MET16 chromatin remodelling and transcription [9].
  • While the deduced amino acid sequence of the sA gene product shows homology with the equivalent MET16 gene product of Saccharomyces cerevisiae, the sC gene product resembles the equivalent MET3 yeast gene product at the N-terminal end, but differs markedly from it at the C-terminal end, showing homology to the APS kinases of several microorganisms [10].
  • Irrespective of the level of transcription, repair at the MspI restriction fragment of MET16 exhibits periodicity in line with nucleosome positions in both strands of the regulatory region and the non-transcribed strand of the coding region [11].

Associations of MET16 with chemical compounds


Other interactions of MET16


  1. Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase structural gene. Thomas, D., Barbey, R., Surdin-Kerjan, Y. J. Biol. Chem. (1990) [Pubmed]
  2. Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription. Morillon, A., Karabetsou, N., Nair, A., Mellor, J. Mol. Cell (2005) [Pubmed]
  3. A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Vignols, F., Bréhélin, C., Surdin-Kerjan, Y., Thomas, D., Meyer, Y. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Interaction of yeast kinetochore proteins with centromere-protein/transcription factor Cbf1. Hemmerich, P., Stoyan, T., Wieland, G., Koch, M., Lechner, J., Diekmann, S. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Role of the Saccharomyces cerevisiae general regulatory factor CP1 in methionine biosynthetic gene transcription. O'Connell, K.F., Surdin-Kerjan, Y., Baker, R.E. Mol. Cell. Biol. (1995) [Pubmed]
  6. Characterization of the redox properties of poplar glutaredoxin. Rouhier, N., Vlamis-Gardikas, A., Lillig, C.H., Berndt, C., Schwenn, J.D., Holmgren, A., Jacquot, J.P. Antioxid. Redox Signal. (2003) [Pubmed]
  7. Inhibition of 5' to 3' mRNA degradation under stress conditions in Saccharomyces cerevisiae: from GCN4 to MET16. Benard, L. RNA (2004) [Pubmed]
  8. Increasing sulphite formation in Saccharomyces cerevisiae by overexpression of MET14 and SSU1. Donalies, U.E., Stahl, U. Yeast (2002) [Pubmed]
  9. Histone acetylation, chromatin remodelling, transcription and nucleotide excision repair in S. cerevisiae: studies with two model genes. Teng, Y., Yu, Y., Ferreiro, J.A., Waters, R. DNA Repair (Amst.) (2005) [Pubmed]
  10. Isolation and characterisation of genes for sulphate activation and reduction in Aspergillus nidulans: implications for evolution of an allosteric control region by gene duplication. Borges-Walmsley, M.I., Turner, G., Bailey, A.M., Brown, J., Lehmbeck, J., Clausen, I.G. Mol. Gen. Genet. (1995) [Pubmed]
  11. Cbf1p modulates chromatin structure, transcription and repair at the Saccharomyces cerevisiae MET16 locus. Ferreiro, J.A., Powell, N.G., Karabetsou, N., Kent, N.A., Mellor, J., Waters, R. Nucleic Acids Res. (2004) [Pubmed]
  12. Sulfur and adenine metabolisms are linked, and both modulate sulfite resistance in wine yeast. Aranda, A., Jiménez-Martí, E., Orozco, H., Matallana, E., Del Olmo, M. J. Agric. Food Chem. (2006) [Pubmed]
  13. Roles for Gcn5p and Ada2p in transcription and nucleotide excision repair at the Saccharomyces cerevisiae MET16 gene. Ferreiro, J.A., Powell, N.G., Karabetsou, N., Mellor, J., Waters, R. Nucleic Acids Res. (2006) [Pubmed]
  14. MET4, a leucine zipper protein, and centromere-binding factor 1 are both required for transcriptional activation of sulfur metabolism in Saccharomyces cerevisiae. Thomas, D., Jacquemin, I., Surdin-Kerjan, Y. Mol. Cell. Biol. (1992) [Pubmed]
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