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  current news   Press   selected story    
     
  22th February  
  Structural basis of Dcp2 recognition and activation by Dcp1
 
 




Authors
Meipei She1, Carolyn J. Decker2, Dmitri I. Svergun3,4, Adam Round3, Nan Chen1, Denise Muhlrad2, Roy Parker2 and Haiwei Song1,5,#

1 Department of Biological Sciences, National University of Singapore, Singapore
2 Institute of Molecular and Cell Biology, Proteos, Singapore
3 Equal first authors
1 Laboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Proteos, Singapore 138673.
2 Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721, USA.
3 Hamburg Outstation, European Molecular Biology Laboratory, Hamburg, Germany
4 Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, 117333 Moscow, Russia
5 Department of Biological Sciences, National University of Singapore, 14 Science Drive, Singapore 117543.

#Correspondence should be addressed to H.S.(haiwei@imcb.a-star.edu.sg).


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 a 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.



Published online in Mol. Cell 14 February 2008;
doi:10.1016/j.molcel.2008.01.002

For more information of HaiWei SONG's Lab, Please Click here.