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Molecular and Cellular Biology, December 2007, p. 8600-8611, Vol. 27, No. 24
0270-7306/07/$08.00+0     doi:10.1128/MCB.01506-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

A Divergent Sm Fold in EDC3 Proteins Mediates DCP1 Binding and P-Body Targeting{triangledown} ,{dagger}

Felix Tritschler, Ana Eulalio, Vincent Truffault, Marcus D. Hartmann, Sigrun Helms, Steffen Schmidt, Murray Coles, Elisa Izaurralde,* and Oliver Weichenrieder*

Max Planck Institute for Developmental Biology, Spemannstrasse 35, D-72076 Tübingen, Germany

Received 19 August 2007/ Returned for modification 18 September 2007/ Accepted 25 September 2007

Members of the (L)Sm (Sm and Sm-like) protein family are found across all kingdoms of life and play crucial roles in RNA metabolism. The P-body component EDC3 (enhancer of decapping 3) is a divergent member of this family that functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a central FDF domain, and a C-terminal YjeF-N domain. We show that this modular architecture enables EDC3 to interact with multiple components of the decapping machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding and P-body localization. We determined the three-dimensional structures of the LSm domains of Drosophila melanogaster and human EDC3 and show that the domain adopts a divergent Sm fold that lacks the characteristic N-terminal {alpha}-helix and has a disrupted ß4-strand. This domain remains monomeric in solution and lacks several features that canonical (L)Sm domains require for binding RNA. The structures also revealed a conserved patch of surface residues that are required for the interaction with DCP1 but not for P-body localization. The conservation of surface and of critical structural residues indicates that LSm domains in EDC3 proteins adopt a similar fold that has separable novel functions that are absent in canonical (L)Sm proteins.

* Corresponding author. Mailing address: Max Planck Institute for Developmental Biology, Spemannstrasse 35, D-72076 Tübingen, Germany. Phone: 49-7071-601-1350. Fax: 49-7071-601-1353. E-mail for Elisa Izaurralde: elisa.izaurralde{at}tuebingen.mpg.de. E-mail for Oliver Weichenrieder: oliver.weichenrieder{at}tuebingen.mpg.de

{triangledown} Published ahead of print on 8 October 2007.

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

Molecular and Cellular Biology, December 2007, p. 8600-8611, Vol. 27, No. 24
0270-7306/07/$08.00+0     doi:10.1128/MCB.01506-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Scofield, D. G., Lynch, M. (2008). Evolutionary Diversification of the Sm Family of RNA-Associated Proteins. Mol Biol Evol 25: 2255-2267 [Abstract] [Full Text]  
  • Ling, S. H. M., Decker, C. J., Walsh, M. A., She, M., Parker, R., Song, H. (2008). Crystal Structure of Human Edc3 and Its Functional Implications. Mol. Cell. Biol. 28: 5965-5976 [Abstract] [Full Text]  
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