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Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1

Vincent Galy1, Olivier Gadal, Micheline Fromont-Racine

  • 1Unité de Biologie Cellulaire du Noyau, CNRS URA 2582, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.

Cell
|January 14, 2004
PubMed

Insights

Nuclear retention of intron-containing mRNAs in yeast is mediated by perinuclear Mlp1 protein. Deleting MLP1 reduces retention, suggesting Mlp1 acts as a nuclear quality control mechanism for mRNA export.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Yeast Genetics

Background:

  • The nuclear retention mechanism for intron-containing mRNAs remains unclear.
  • Understanding mRNA processing and export is crucial for gene expression regulation.

Purpose of the Study:

  • To elucidate the molecular mechanism of intron-containing mRNA nuclear retention in yeast.
  • To identify key proteins involved in regulating mRNA export.

Main Methods:

  • Gene deletion studies in yeast (MLP1, RRP6).
  • Analysis of mRNA splicing and nuclear retention.
  • Investigation of splicing mutants (ts-prp18 delta).
  • Localization studies of Mlp1 protein.

Main Results:

  • Perinuclear Mlp1 mediates the retention of intron-containing mRNAs.
  • MLP1 deletion impairs retention without affecting splicing efficiency.
  • Mlp1-dependent RNA leakage is exacerbated in splicing mutants and when nuclear exosome function is compromised.
  • Retention is linked to the 5' splice site, and Mlp1 localizes to chromatin-associated nuclear envelope regions.

Conclusions:

  • Perinuclear Mlp1 functions as a critical quality control factor, retaining faulty pre-mRNAs at the nuclear envelope before export.
  • This mechanism ensures the fidelity of mRNA export and subsequent protein synthesis.

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