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A novel mode of RBD-protein recognition in the Y14-Mago complex

Sébastien Fribourg1, David Gatfield, Elisa Izaurralde

  • 1European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.

Nature Structural Biology
|May 6, 2003
PubMed

Insights

The crystal structure reveals how Y14 and Mago proteins bind, crucial for mRNA quality control and localization. Their interaction is essential for the nonsense-mediated mRNA decay (NMD) pathway.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Y14 and Mago are conserved eukaryotic proteins associated with spliced mRNAs.
  • They play roles in mRNA quality control, including nonsense-mediated mRNA decay (NMD), and mRNA localization.

Purpose of the Study:

  • To determine the crystal structure of the Y14-Mago complex.
  • To elucidate the molecular mechanism of Y14-Mago interaction and its role in the NMD pathway.

Main Methods:

  • X-ray crystallography to determine the structure of the Drosophila melanogaster Y14-Mago complex at 2.5 Å resolution.
  • Structure-guided mutagenesis to investigate the functional significance of the Y14-Mago interaction in the NMD pathway.

Main Results:

  • The crystal structure revealed an atypical protein-protein interaction mediated by Y14's RNA-binding domain (RBD).
  • Y14's RBD, instead of binding RNA, uses its RNP1 and RNP2 motifs to bind Mago.
  • Mago was confirmed as a component of the NMD pathway, with its association with Y14 being essential for function.

Conclusions:

  • The Y14-Mago complex forms a structural platform for interaction with the NMD machinery.
  • Phylogenetically conserved residues mediate the interaction with the NMD machinery, highlighting evolutionary conservation of the pathway.
  • The findings provide structural insights into mRNA quality control mechanisms involving Y14 and Mago proteins.

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