Nuclear mRNA surveillance in THO/sub2 mutants is triggered by inefficient polyadenylation.

The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay.

Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants.

The nuclear exosome is involved in numerous RNA metabolic processes. Exosome degradation of rRNA, snoRNA, snRNA and tRNA in Saccharomyces cerevisiae is activated by TRAMP complexes, containing either the Trf4p or Trf5p poly(A) polymerase. These enzymes are presumed to facilitate exosome access by appending oligo(A)-tails onto structured substrates.

A link between transcription and mRNP quality in Saccharomyces cerevisiae.

The transcription machinery plays a direct role in the assembly of messenger ribonucleoprotein particles (mRNPs), contributing to the loading of proteins onto nascent transcripts. Such mRNP biogenesis is linked to the THO complex that operates at the boundary between transcription and nuclear export. Early mRNP assembly events are subject to surveillance by the nuclear exosome that retains, and degrades, aberrant mRNAs.

Formation of export-competent mRNP: escaping nuclear destruction.

In eukaryotic cells, primary transcripts are processed and bound by proteins before export to the cytoplasm. Nuclear production of export-competent messenger ribonucleoprotein particles (mRNPs) is a complicated process, and mRNP biogenic events that function sub-optimally are rapidly attacked by surveillance leading to degradation of the mRNA. Export of nuclear mRNAs is therefore constantly challenged by the opposing force of mRNA retention and decay.

Modulation of transcription affects mRNP quality.

Cotranscriptional loading of proteins onto nascent transcripts contributes to the formation of messenger ribonucleoprotein particles (mRNPs) competent for nuclear export. The transcription machinery is believed to play a pivotal role in mRNP assembly, which is at least partially linked to the function of the THO/TREX complex and the mRNA termination/polyadenylation apparatus. Here we demonstrate a prominent role for the rate of transcription in the production of export-competent mRNPs.