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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Molecular basis for GIGYF-TNRC6 complex assembly.

Meghna Sobti1,2, Benjamin J Mead3, Alastair G Stewart1,2

  • 1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Sydney, New South Wales 2010, Australia.

RNA (New York, N.Y.)
|February 28, 2023
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Researchers elucidated how GIGYF proteins bind target RNAs. Structural analysis reveals TNRC6 proteins bridge GIGYF-4EHP complexes to Argonaute, mediating transcript-specific translational repression.

Keywords:
X-ray crystallographygene regulationsilencingtranslational repression

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • RNA Biology

Background:

  • GIGYF proteins and 4EHP mediate transcript-specific translational repression.
  • The recruitment mechanism of the GIGYF1/2-4EHP complex to target transcripts is not fully understood.

Purpose of the Study:

  • To determine the structural basis for GIGYF1/2-4EHP complex recruitment to target RNAs.
  • To elucidate the role of TNRC6 proteins in bridging GIGYF proteins to Argonaute-miRNA complexes.

Main Methods:

  • X-ray crystallography was used to determine the structures of GIGYF1 and GIGYF2 GYF domains.
  • Complexes were formed with proline-rich sequences from TNRC6C and TNRC6A proteins.

Main Results:

  • Crystal structures revealed TNRC6 proline-rich motifs binding to conserved aromatic residues on GIGYF1/2 GYF domains.
  • This interaction bridges the 4EHP protein to Argonaute-miRNA complexes, facilitating translational repression.
  • A conserved phenylalanine residue was identified that enhances GIGYF2 thermostability.

Conclusions:

  • The study provides molecular details for GIGYF-mediated translational repression.
  • These findings are likely conserved across species and in other RNA-binding proteins involved in translational control.