THO/Sub2p functions to coordinate 3'-end processing with gene-nuclear pore association

Cell. 2008 Oct 17;135(2):308-21. doi: 10.1016/j.cell.2008.08.005.


During transcription, proteins assemble sequentially with nascent RNA to generate a messenger ribonucleoprotein particle (mRNP). The THO complex and its associated Sub2p helicase are functionally implicated in both transcription and mRNP biogenesis but their precise function remains elusive. We show here that THO/Sub2p mutation leads to the accumulation of a stalled intermediate in mRNP biogenesis that contains nuclear pore components and polyadenylation factors in association with chromatin. Microarray analyses of genomic loci that are aberrantly docked to the nuclear pore in mutants allowed the identification of approximately 400 novel validated target genes that require THO /Sub2p for efficient expression. Our data strongly suggests that the THO complex/Sub2p function is required to coordinate events leading to the acquisition of export competence at a step that follows commitment to 3'-processing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Chromatin / metabolism
  • Heat-Shock Proteins / genetics
  • Mutation
  • Nuclear Pore / metabolism*
  • Nuclear Proteins / metabolism
  • Nucleocytoplasmic Transport Proteins / metabolism
  • Nucleosomes / metabolism
  • RNA 3' End Processing*
  • RNA Polymerase II / metabolism
  • RNA Transport*
  • RNA, Fungal / metabolism
  • RNA-Binding Proteins / metabolism
  • Ribonucleoproteins / metabolism
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription, Genetic


  • Chromatin
  • Heat-Shock Proteins
  • MEX67 protein, S cerevisiae
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Nucleosomes
  • RNA, Fungal
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • HsP104 protein, S cerevisiae
  • RNA Polymerase II
  • Adenosine Triphosphatases
  • RNA-dependent ATPase