Structural highlights
Publication Abstract from PubMed
Elimination of the 5' cap of eukaryotic mRNAs, known as decapping, is considered to be a crucial, irreversible and highly regulated step required for the rapid degradation of mRNA by Xrn1, the major cytoplasmic 5'-3' exonuclease. Decapping is accomplished by the recruitment of a protein complex formed by the Dcp2 catalytic subunit and its Dcp1 cofactor. However, this complex has a low intrinsic enzymatic activity and requires several accessory proteins such as the Lsm1-7 complex, Pat1, Edc1-Edc2 and/or Edc3 to be fully active. Here we present the crystal structure of the active form of the yeast Kluyveromyces lactis Dcp1-Dcp2 enzyme bound to its product (m7GDP) and its potent activator Edc3. This structure of the Dcp1-Dcp2 complex bound to a cap analog further explains previously published data on substrate binding and provides hints as to the mechanism of Edc3-mediated Dcp2 activation.
Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator.,Charenton C, Taverniti V, Gaudon-Plesse C, Back R, Seraphin B, Graille M Nat Struct Mol Biol. 2016 Oct 3. doi: 10.1038/nsmb.3300. PMID:27694841[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Charenton C, Taverniti V, Gaudon-Plesse C, Back R, Seraphin B, Graille M. Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator. Nat Struct Mol Biol. 2016 Oct 3. doi: 10.1038/nsmb.3300. PMID:27694841 doi:http://dx.doi.org/10.1038/nsmb.3300
