The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

DCS2  -  Dcs2p

Saccharomyces cerevisiae S288c

Synonyms: Histidine triad protein, Inactive diphosphatase DCS2, O3625, Protein Dcs2p, YOR173W
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on DCS2

  • Hint, histidine triad nucleotide-binding protein, is a universally conserved enzyme that hydrolyzes AMP linked to lysine and, in yeast, functions as a positive regulator of the RNA polymerase II C-terminal domain kinase, Kin28 [1].
  • We have characterized a new type of histidine triad (HIT) motif protein (Nhm1) that co-purifies with the cap-binding complex eIF4F of Schizosaccharomyces pombe [2].
  • The resulting Dcs2 protein forms a heterodimer together with Dcs1, both modulating Dcs1 substrate specificity and suppressing its k(cat) [3].
  • In contrast to these findings, parallel studies with a polyclonal antibody to FHIT, a related histidine triad (HIT) protein and putative tumor suppressor, indicated that FHIT was expressed at low or undetectable levels in some of the same cell lines [4].
  • Nutrient stress induces DCS1 and DCS2 transcription via the cAMP-PKA signalling pathway [5].
 

Associations of DCS2 with chemical compounds

  • We now show that the absence of Dcs1, and the closely related Dcs2 protein, compromises cellular responses to glucose-deprivation stress as well as to step changes in glucose availability [5].
 

Analytical, diagnostic and therapeutic context of DCS2

  • Sequence alignments of DcpS from different organisms revealed the presence of a conserved hexapeptide, containing a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues [6].

References

  1. Biochemical, crystallographic, and mutagenic characterization of hint, the AMP-lysine hydrolase, with novel substrates and inhibitors. Krakowiak, A., Pace, H.C., Blackburn, G.M., Adams, M., Mekhalfia, A., Kaczmarek, R., Baraniak, J., Stec, W.J., Brenner, C. J. Biol. Chem. (2004) [Pubmed]
  2. A nuclear protein in Schizosaccharomyces pombe with homology to the human tumour suppressor Fhit has decapping activity. Salehi, Z., Geffers, L., Vilela, C., Birkenhäger, R., Ptushkina, M., Berthelot, K., Ferro, M., Gaskell, S., Hagan, I., Stapley, B., McCarthy, J.E. Mol. Microbiol. (2002) [Pubmed]
  3. Dcs2, a Novel Stress-induced Modulator of m(7)GpppX Pyrophosphatase Activity that Locates to P Bodies. Malys, N., McCarthy, J.E. J. Mol. Biol. (2006) [Pubmed]
  4. Characterization of PKCI and comparative studies with FHIT, related members of the HIT protein family. Klein, M.G., Yao, Y., Slosberg, E.D., Lima, C.D., Doki, Y., Weinstein, I.B. Exp. Cell Res. (1998) [Pubmed]
  5. The 'scavenger' m7GpppX pyrophosphatase activity of Dcs1 modulates nutrient-induced responses in yeast. Malys, N., Carroll, K., Miyan, J., Tollervey, D., McCarthy, J.E. Nucleic Acids Res. (2004) [Pubmed]
  6. The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. Liu, H., Rodgers, N.D., Jiao, X., Kiledjian, M. EMBO J. (2002) [Pubmed]
 
WikiGenes - Universities