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

The molecular mechanism underlying the retention of intron-containing mRNAs in the nucleus is not understood. Here, we show that retention of intron-containing mRNAs in yeast is mediated by perinuclearly located Mlp1. Deletion of MLP1 impairs retention while having no effect on mRNA splicing. The Mlp1-dependent leakage of intron-containing RNAs is increased in presence of ts-prp18 delta, a splicing mutant. When overall pre-mRNA levels are increased by deletion of RRP6, a nuclear exosome component, MLP1 deletion augments leakage of only the intron-containing portion of mRNAs. Our data suggest, moreover, that Mlp1-dependent retention is mediated via the 5' splice site. Intriguingly, we found Mlp-proteins to be present only on sections of the NE adjacent to chromatin. We propose that at this confined site the perinuclear Mlp1 implements a quality control step prior to export, physically retaining faulty pre-mRNAs.

Pubmed ID: 14718167

Authors

  • Galy V
  • Gadal O
  • Fromont-Racine M
  • Romano A
  • Jacquier A
  • Nehrbass U

Journal

Cell

Publication Data

January 9, 2004

Associated Grants

None

Mesh Terms

  • Active Transport, Cell Nucleus
  • Cell Nucleus
  • Exoribonucleases
  • Exosome Multienzyme Ribonuclease Complex
  • Introns
  • Mutation
  • Nuclear Envelope
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Protein Transport
  • RNA Splice Sites
  • RNA Splicing
  • RNA, Messenger
  • Ribonucleoprotein, U5 Small Nuclear
  • Saccharomyces cerevisiae Proteins
  • Yeasts