Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 11, Pages 982-986Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3300
Keywords
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Funding
- Ecole Polytechnique
- Centre National pour la Recherche Scientifique - ATIP-AVENIR program
- Agence Nationale pour la Recherche [ANR-11-BSV8-009, ANR-10-LABX-0030-INRT, ANR-10-IDEX-0002-02]
- Ligue Contre le Cancer (Equipe Labellisee)
- CERBM-IGBMC
- INSERM
- French Ministere de l'Enseignement Superieur et de la Recherche (MESR)
- ENS Cachan
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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 (m(7)GDP) 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.
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