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Molecular basis for GIGYF-TNRC6 complex assembly

MPG-Autoren
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Igreja,  C       
Department Integrative Evolutionary Biology, 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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Zitation

Sobti, M., Mead, B., Stewart, A., Igreja, C., & Christie, M. (2023). Molecular basis for GIGYF-TNRC6 complex assembly. RNA: A Publication of the RNA Society, 29(6), 724-734. doi:10.1261/rna.079596.123.


Zitierlink: https://hdl.handle.net/21.11116/0000-000A-62B5-B
Zusammenfassung
The GIGYF proteins interact with 4EHP and RNA-associated proteins to elicit transcript-specific translational repression. However, the mechanism by which the GIGYF1/2-4EHP complex is recruited to its target transcripts remain unclear. Here we report the crystal structures of the GYF domains from GIGYF1 and GIGYF2 in complex with proline-rich sequences from miRISC-binding proteins TNRC6C and TNRC6A, respectively. The TNRC6 proline-rich motifs bind to a conserved array of aromatic residues on the surface of the GIGYF1/2 GYF domain, thereby bridging 4EHP to Argonaute-miRNA complexes. Our structures also reveal a phenylalanine residue conserved from yeast to human GYF domains that contributes to GIGYF2 thermostability. The molecular details we outline here are likely to be conserved between GIGYF1/2 and other RNA-binding proteins to elicit 4EHP-mediated repression in different biological contexts.