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Journal Article

DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa

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

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Braun,  JE
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Motz,  C
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Igreja,  C
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;
Regulation and Post-Translational Modification of Gene Expression in Nematodes Group, Department Integrative Evolutionary Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

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Haas,  G
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Truffault,  V
Department Biochemistry, 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., Braun, J., Motz, C., Igreja, C., Haas, G., Truffault, V., et al. (2009). DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa. Proceedings of the National Academy of Sciences of the United States of America, 106(51), 21591-21596. doi:10.1073/pnas.0909871106.


Cite as: https://hdl.handle.net/21.11116/0000-000A-E2BF-0
Abstract
DCP1 stimulates the decapping enzyme DCP2, which removes the mRNA 5' cap structure committing mRNAs to degradation. In multicellular eukaryotes, DCP1-DCP2 interaction is stabilized by additional proteins, including EDC4. However, most information on DCP2 activation stems from studies in S. cerevisiae, which lacks EDC4. Furthermore, DCP1 orthologs from multicellular eukaryotes have a C-terminal extension, absent in fungi. Here, we show that in metazoa, a conserved DCP1 C-terminal domain drives DCP1 trimerization. Crystal structures of the DCP1-trimerization domain reveal an antiparallel assembly comprised of three kinked alpha-helices. Trimerization is required for DCP1 to be incorporated into active decapping complexes and for efficient mRNA decapping in vivo. Our results reveal an unexpected connectivity and complexity of the mRNA decapping network in multicellular eukaryotes, which likely enhances opportunities for regulating mRNA degradation.