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Updated: Aug 31, 2025

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
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Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex

Anne-Emmanuelle Foucher1, Leila Touat-Todeschini2, Ariadna B Juarez-Martinez1

  • 1Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000, Grenoble, France.

Nature Communications
|August 24, 2022
PubMed

Insights

Nuclear RNA degradation complexes MTREC and PAXT are crucial for cellular function. Structural and in vivo studies reveal conserved mechanisms and dimerization of key proteins, providing insights into their architecture and function in RNA processing.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Eukaryotes utilize nuclear RNA-targeting complexes to degrade specific or aberrant transcripts via the exosome.
  • The S. pombe MTREC and human PAXT complexes are key players in this RNA degradation pathway.
  • Detailed understanding of the inner workings of these complexes remains limited.

Purpose of the Study:

  • To elucidate the structural mechanisms and conserved features of the MTREC and PAXT RNA degradation complexes.
  • To investigate the interactions between key protein components of these complexes.
  • To provide mechanistic insights into the architecture and function of MTREC/PAXT.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the structure of the Red1 helix-turn-helix domain bound to Iss10.
  • X-ray crystallography to determine the structure of the Red1-Ars2 complex.
  • In vivo studies to assess the functional significance of observed interactions and dimerization.

Main Results:

  • NMR structure reveals Red1-Iss10 interaction essential for cellular growth and meiotic mRNA degradation.
  • Crystal structure of Red1-Ars2 complex explains mutually exclusive interactions with RNA regulators.
  • Both Red1 and hZFC3H1 were shown to homo-dimerize, suggesting MTREC and PAXT function as dimers.

Conclusions:

  • Structural and functional data provide mechanistic insights into conserved features of MTREC/PAXT architecture.
  • The findings highlight the importance of specific protein-protein interactions and dimerization in RNA degradation.
  • This study advances the understanding of eukaryotic nuclear RNA processing and quality control mechanisms.

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