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LARP1 binds ribosomes and TOP mRNAs in repressed complexes.

James A Saba1,2, Zixuan Huang3, Kate L Schole1,2

  • 1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.

The EMBO Journal
|November 12, 2024
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Summary
This summary is machine-generated.

LARP1 directly binds ribosomal subunits, not translating ribosomes, to regulate ribosomal protein mRNAs (TOPs). This challenges current models of LARP1-mediated TOP repression and stabilization.

Keywords:
Cryo-EMLARP1RibosomeTOP mRNATranslation

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Terminal oligopyrimidine motif-containing mRNAs (TOPs) encode ribosomal proteins and are crucial for regulating ribosome synthesis.
  • LARP1 has been implicated in repressing and stabilizing TOPs through interactions with 40S- or 80S-ribosome complexes, but the molecular mechanisms are unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which LARP1 interacts with ribosomal subunits and TOP mRNAs.
  • To investigate the role of LARP1-ribosome complexes in TOP mRNA regulation.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) to determine the structure of LARP1-ribosome complexes.
  • Biochemical assays to study LARP1 binding to ribosomal subunits and TOPs.

Main Results:

  • LARP1 directly binds to non-translating 40S ribosomal subunits via a novel domain, occluding the mRNA channel.
  • LARP1 forms 80S complexes with TOPs upon increased availability of free ribosomal subunits during stress.
  • Ribosome binding is not essential for LARP1's known functions in TOP repression and stabilization.

Conclusions:

  • LARP1 directly binds ribosomal subunits, offering a new perspective on its regulatory role.
  • Existing models of LARP1-mediated TOP regulation via repressed 40S/80S-TOP complexes need revision.
  • This study provides critical molecular insights into LARP1-ribosome interactions and TOP mRNA regulation.