A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting

Tritschler, F; Eulalio, A; Truffault, V; Hartmann, MD; Helms, S; Schmidt, S; Coles, M; Izaurralde, E; Weichenrieder, O

doi:10.1128/MCB.01506-07

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A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting

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Tritschler, F
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Eulalio, A
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Truffault, V
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hartmann, MD
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Helms, S
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Schmidt, S
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Coles, M
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Izaurralde, E
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Weichenrieder, O
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;
Retrotransposition and Regulatory RNAs Group, Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Tritschler, F., Eulalio, A., Truffault, V., Hartmann, M., Helms, S., Schmidt, S., et al. (2007). A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. Molecular and Cellular Biology (Washington, DC), 27(24), 8600-8611. doi:10.1128/MCB.01506-07.

Cite as: https://hdl.handle.net/21.11116/0000-000A-F2F8-D

Abstract

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 beta4-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.