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Structure of the Dcp2–Dcp1 mRNA-decapping complex in the activated conformation

DOI: 10.1038/nsmb.3232 DOI Help

Authors: Eugene Valkov (Max Planck Institute for Developmental Biology, Tübingen, German) , Sowndarya Muthukumar (Max Planck Institute for Developmental Biology) , Chung-te Chang (Max Planck Institute for Developmental Biology, Tübingen, Germany) , Stefanie Jonas (Max Planck Institute for Developmental Biology, Tübingen, Germany) , Oliver Weichenrieder (Max Planck Institute for Developmental Biology, Tübingen, Germany) , Elisa Izaurralde (Max Planck Institute for Developmental Biology, Tübingen, Germany)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 23 , PAGES 574 - 579

State: Published (Approved)
Published: May 2016

Open Access Open Access

Abstract: The removal of the mRNA 5′ cap (decapping) by Dcp2 shuts down translation and commits mRNA to full degradation. Dcp2 activity is enhanced by activator proteins such as Dcp1 and Edc1. However, owing to conformational flexibility, the active conformation of Dcp2 and the mechanism of decapping activation have remained unknown. Here, we report a 1.6-Å-resolution crystal structure of the Schizosaccharomyces pombe Dcp2–Dcp1 heterodimer in an unprecedented conformation that is tied together by an intrinsically disordered peptide from Edc1. In this ternary complex, an unforeseen rotation of the Dcp2 catalytic domain allows residues from both Dcp2 and Dcp1 to cooperate in RNA binding, thus explaining decapping activation by increased substrate affinity. The architecture of the Dcp2–Dcp1–Edc1 complex provides a rationale for the conservation of a sequence motif in Edc1 that is also present in unrelated decapping activators, thus indicating that the presently described mechanism of decapping activation is evolutionarily conserved.

Subject Areas: Biology and Bio-materials


Instruments: B21-High Throughput SAXS

Other Facilities: PX beamlines of the Swiss Light Source

Added On: 12/07/2016 15:26

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nsmb.3232.pdf

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