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Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation

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Peter,  D
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Weber,  R
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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

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Chung,  M-Y
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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

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Citation

Peter, D., Weber, R., Köne, C., Chung, M.-Y., Ebertsch, L., Truffault, V., et al. (2015). Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation. Genes and Development, 29(17), 1835-1849. doi:10.1101/gad.269068.115.


Cite as: https://hdl.handle.net/21.11116/0000-000A-A085-A
Abstract
The eIF4E-binding proteins (4E-BPs) are a diverse class of translation regulators that share a canonical eIF4E-binding motif (4E-BM) with eIF4G. Consequently, they compete with eIF4G for binding to eIF4E, thereby inhibiting translation initiation. Mextli (Mxt) is an unusual 4E-BP that promotes translation by also interacting with eIF3. Here we present the crystal structures of the eIF4E-binding regions of the Drosophila melanogaster (Dm) and Caenorhabditis elegans (Ce) Mxt proteins in complex with eIF4E in the cap-bound and cap-free states. The structures reveal unexpected evolutionary plasticity in the eIF4E-binding mode, with a classical bipartite interface for Ce Mxt and a novel tripartite interface for Dm Mxt. Both interfaces comprise a canonical helix and a noncanonical helix that engage the dorsal and lateral surfaces of eIF4E, respectively. Remarkably, Dm Mxt contains a C-terminal auxiliary helix that lies anti-parallel to the canonical helix on the eIF4E dorsal surface. In contrast to the eIF4G and Ce Mxt complexes, the Dm eIF4E-Mxt complexes are resistant to competition by bipartite 4E-BPs, suggesting that Dm Mxt can bind eIF4E when eIF4G binding is inhibited. Our results uncovered unexpected diversity in the binding modes of 4E-BPs, resulting in eIF4E complexes that display differential sensitivity to 4E-BP regulation.