Structural Basis of Dcp2 Recognition and Activation by Dcp1

Overview

Journal Mol Cell

Publisher Cell Press

Specialty Cell Biology

Date 2008 Feb 19

PMID 18280239

Citations 86

Authors

Meipei She

Carolyn J Decker

Dmitri I Svergun

Adam Round

Nan Chen

Denise Muhlrad

Roy Parker

Haiwei Song

Affiliations

Soon will be listed here.

Abstract

A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor.

Citing Articles

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