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Gene Review

DCP2  -  Dcp2p

Saccharomyces cerevisiae S288c

Synonyms: N1917, PSU1, Protein PSU1, YNL118C, mRNA-decapping enzyme subunit 2
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Disease relevance of DCP2

  • To determine the function of both Dcp1p and Dcp2p in decapping, we purified recombinant versions of these proteins from Escherichia coli and examined their properties [1].

High impact information on DCP2

  • Subsequent recruitment of Dcp1p/Dcp2p to the complex appears to ensure rapid, deadenylation-independent decapping of the mRNA [2].
  • In yeast, Dcp1p, Dcp2p, Lsm1-7p, and Xrn1p are required for mRNA decay and are localized within discrete cytoplasmic foci; in the May 2 issue of Science, Sheth and Parker provide compelling evidence that these foci represent sites for mRNA decay [3].
  • Taken together these data suggest that in yeast, PSU1 is involved in ligand-dependent transactivation by NRs [4].
  • Role of the essential yeast protein PSU1 in p6anscriptional enhancement by the ligand-dependent activation function AF-2 of nuclear receptors [4].
  • Consistent with their role in mRNA decay, DCP1, DCP2, and VCS colocalize in cytoplasmic foci, which are putative Arabidopsis processing bodies [5].

Biological context of DCP2

  • These results suggest that direct or indirect interaction of Dcp1p with Dcp2p is required for the production of active decapping enzyme, perhaps in a process requiring the hydrolysis of a pyrophosphate bond [6].
  • One of the rate-limiting steps in messenger RNA decay pathway is the 5'-cap cleavage of mRNAs, decapping reaction, which is conducted by the protein complex of Dcp1 and Dcp2 [7].
  • Sequence analysis revealed that in addition to a highly conserved motif found in a family of MutT-related proteins, PSU1 contains several alpha-helical leucine-rich motifs sharing the consensus sequence LLxPhiL (x, any amino acid; Phi, hydrophobic amino acid) in regions that elicit either transactivation or NR-binding activity [4].
  • Here we show that Caenorhabditis elegans Dcp2 is localized to distinct foci during embryogenesis, reminiscent of P-bodies, the sites of mRNA degradation in yeast and mammals [8].
  • This suggests that Dcp1p/Dcp2p contains an additional RNA-binding site spatially distinct from the active site [1].

Physical interactions of DCP2

  • The Dcp2p also coimmunoprecipitates with the DCP1 decapping enzyme and is required for the production of enzymatically active decapping enzyme [6].
  • Evidence is presented here that Rpm2p interacts with Dcp2p, a subunit of mRNA decapping enzyme in the two-hybrid assay, and is enriched in cytoplasmic P bodies, the sites of mRNA degradation and storage in yeast and mammalian cells [9].

Other interactions of DCP2


  1. Analysis of recombinant yeast decapping enzyme. Steiger, M., Carr-Schmid, A., Schwartz, D.C., Kiledjian, M., Parker, R. RNA (2003) [Pubmed]
  2. Regulation of mRNA decay: decapping goes solo. Jacobson, A. Mol. Cell (2004) [Pubmed]
  3. mRNA decay: x (XRN1) marks the spot. Long, R.M., McNally, M.T. Mol. Cell (2003) [Pubmed]
  4. Role of the essential yeast protein PSU1 in p6anscriptional enhancement by the ligand-dependent activation function AF-2 of nuclear receptors. Gaudon, C., Chambon, P., Losson, R. EMBO J. (1999) [Pubmed]
  5. Arabidopsis DCP2, DCP1, and VARICOSE Form a Decapping Complex Required for Postembryonic Development. Xu, J., Yang, J.Y., Niu, Q.W., Chua, N.H. Plant Cell (2006) [Pubmed]
  6. The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. Dunckley, T., Parker, R. EMBO J. (1999) [Pubmed]
  7. The decapping enzyme Dcp1 participates in translation termination through its interaction with the release factor eRF3 in budding yeast. Kofuji, S., Sakuno, T., Takahashi, S., Araki, Y., Doi, Y., Hoshino, S., Katada, T. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  8. Caenorhabditis elegans decapping proteins: localization and functional analysis of Dcp1, Dcp2, and DcpS during embryogenesis. Lall, S., Piano, F., Davis, R.E. Mol. Biol. Cell (2005) [Pubmed]
  9. Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies. Stribinskis, V., Ramos, K.S. Nucleic Acids Res. (2007) [Pubmed]
  10. Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Dunckley, T., Tucker, M., Parker, R. Genetics (2001) [Pubmed]
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