Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational 
repression

Peter, D; Ruscica, V; Bawankar, P; Weber, R; Helms, S; Valkov, E; Igreja, C; Izaurralde, E

doi:10.1101/gad.329219.119

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Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression

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

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Ruscica, V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273085

Bawankar, P
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons272040

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

/persons/resource/persons273078

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

/persons/resource/persons272049

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

/persons/resource/persons271538

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;

/persons/resource/persons271767

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

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Citation

Peter, D., Ruscica, V., Bawankar, P., Weber, R., Helms, S., Valkov, E., et al. (2019). Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression. Genes and Development, 33(19-20), 1355-1360. doi:10.1101/gad.329219.119.

Cite as: https://hdl.handle.net/21.11116/0000-000A-6715-B

Abstract

GIGYF (Grb10-interacting GYF [glycine-tyrosine-phenylalanine domain]) proteins coordinate with 4EHP (eIF4E [eukaryotic initiation factor 4E] homologous protein), the DEAD (Asp-Glu-Ala-Asp)-box helicase Me31B/DDX6, and mRNA-binding proteins to elicit transcript-specific repression. However, the underlying molecular mechanism remains unclear. Here, we report that GIGYF contains a motif necessary and sufficient for direct interaction with Me31B/DDX6. A 2.4 Å crystal structure of the GIGYF-Me31B complex reveals that this motif arranges into a coil connected to a β hairpin on binding to conserved hydrophobic patches on the Me31B RecA2 domain. Structure-guided mutants indicate that 4EHP-GIGYF-DDX6 complex assembly is required for tristetraprolin-mediated down-regulation of an AU-rich mRNA, thus revealing the molecular principles of translational repression.