Skip to Content
Merck
CN
  • Degradation of Non-coding RNAs Promotes Recycling of Termination Factors at Sites of Transcription.

Degradation of Non-coding RNAs Promotes Recycling of Termination Factors at Sites of Transcription.

Cell reports (2020-07-23)
Tommaso Villa, Mara Barucco, Maria-Jose Martin-Niclos, Alain Jacquier, Domenico Libri
ABSTRACT

A large share of the non-coding transcriptome in yeast is controlled by the Nrd1-Nab3-Sen1 (NNS) complex, which promotes transcription termination of non-coding RNA (ncRNA) genes, and by the nuclear exosome, which limits the steady-state levels of the transcripts produced. How unconstrained ncRNA levels affect RNA metabolism and gene expression are long-standing and important questions. Here, we show that degradation of ncRNAs by the exosome is required for freeing Nrd1 and Nab3 from the released transcript after termination. In exosome mutants, these factors are sequestered by ncRNAs and cannot be efficiently recycled to sites of transcription, inducing termination defects at NNS targets. ncRNA-dependent, genome-wide termination defects can be recapitulated by the expression of a degradation-resistant, circular RNA containing a natural NNS target in exosome-proficient cells. Our results have important implications for the mechanism of termination, the general impact of ncRNAs abundance, and the importance of nuclear ncRNA degradation.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
2-Chloro-5-iodobenzoic acid, 97%
Sigma-Aldrich
Monoclonal Anti-polyHistidine antibody produced in mouse, clone HIS-1, ascites fluid
Sigma-Aldrich
Ribonuclease Inhibitor, Human, Recombinant, E. coli, The Ribonuclease Inhibitor, Human, Recombinant, E. coli controls the biological activity of Ribonuclease. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.
Sigma-Aldrich
Peroxidase Anti-Peroxidase Soluble Complex antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
IgG from rabbit serum, reagent grade, ≥95% (SDS-PAGE), essentially salt-free, lyophilized powder
Sigma-Aldrich
Guanidine hydrochloride, organic base and chaeotropic agent, ≥99% (titration)