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Molecular and Cellular Biology, October 2008, p. 5965-5976, Vol. 28, No. 19
0270-7306/08/$08.00+0     doi:10.1128/MCB.00761-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Crystal Structure of Human Edc3 and Its Functional Implications{triangledown} ,{dagger}

Sharon H. M. Ling,1 Carolyn J. Decker,2 Martin A. Walsh,3 Meipei She,1 Roy Parker,2 and Haiwei Song1*

Laboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore,1 Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, Arizona 85721,2 MRC France, CRG BM14, ESRF, B.P. 220, F-38043, Grenoble CEDEX, France3

Received 12 May 2008/ Returned for modification 10 June 2008/ Accepted 17 July 2008

Edc3 is an enhancer of decapping and serves as a scaffold that aggregates mRNA ribonucleoproteins together for P-body formation. Edc3 forms a network of interactions with the components of the mRNA decapping machinery and has a modular domain architecture consisting of an N-terminal Lsm domain, a central FDF domain, and a C-terminal YjeF-N domain. We have determined the crystal structure of the N-terminally truncated human Edc3 at a resolution of 2.2 Å. The structure reveals that the YjeF-N domain of Edc3 possesses a divergent Rossmann fold topology that forms a dimer, which is supported by sedimentation velocity and sedimentation equilibrium analysis in solution. The dimerization interface of Edc3 is highly conserved in eukaryotes despite the overall low sequence homology across species. Structure-based site-directed mutagenesis revealed dimerization is required for efficient RNA binding, P-body formation, and likely for regulating the yeast Rps28B mRNA as well, suggesting that the dimeric form of Edc3 is a structural and functional unit in mRNA degradation.

* Corresponding author. Mailing address: Laboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore. Phone: 65-6586 9700. Fax: 65-6779 1117. E-mail: haiwei{at}imcb.a-star.edu.sg

{triangledown} Published ahead of print on 4 August 2008.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, October 2008, p. 5965-5976, Vol. 28, No. 19
0270-7306/08/$08.00+0     doi:10.1128/MCB.00761-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bond, C. S., Fox, A. H. (2009). Paraspeckles: nuclear bodies built on long noncoding RNA. JCB 186: 637-644 [Abstract] [Full Text]  
  • Tritschler, F., Eulalio, A., Helms, S., Schmidt, S., Coles, M., Weichenrieder, O., Izaurralde, E., Truffault, V. (2008). Similar Modes of Interaction Enable Trailer Hitch and EDC3 To Associate with DCP1 and Me31B in Distinct Protein Complexes. Mol. Cell. Biol. 28: 6695-6708 [Abstract] [Full Text]  


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