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Structural basis of dcp2 recognition and activation by dcp1.

Authors :
She M
Decker CJ
Svergun DI
Round A
Chen N
Muhlrad D
Parker R
Song H
Source :
Molecular cell [Mol Cell] 2008 Feb 15; Vol. 29 (3), pp. 337-49.
Publication Year :
2008

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.

Details

Language :
English
ISSN :
1097-2765
Volume :
29
Issue :
3
Database :
MEDLINE
Journal :
Molecular cell
Publication Type :
Academic Journal
Accession number :
18280239
Full Text :
https://doi.org/10.1016/j.molcel.2008.01.002