Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 19, Issue 12, Pages 1324-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2413
Keywords
-
Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft (DFG) [FOR855]
- Gottfried Wilhelm Leibniz Program
Ask authors/readers for more resources
The removal of the mRNA 5' cap structure by the decapping enzyme DCP2 leads to rapid 5'-> 3' mRNA degradation by XRN1, suggesting that the two processes are coordinated, but the coupling mechanism is unknown. DCP2 associates with the decapping activators EDC4 and DCP1. Here we show that XRN1 directly interacts with EDC4 and DCP1 in human and Drosophila melanogaster cells, respectively. In D. melanogaster cells, this interaction is mediated by the DCP1 EVH1 domain and a DCP1-binding motif (DBM) in the XRN1 C-terminal region. The NMR structure of the DCP1 EVH1 domain bound to the DBM reveals that the peptide docks at a conserved aromatic cleft, which is used by EVH1 domains to recognize proline-rich ligands. Our findings reveal a role for XRN1 in decapping and provide a molecular basis for the coupling of decapping to 5'-> 3' mRNA degradation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available