ArticleNucleic acids research2008
Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
67 citing papers in PubMed, 93 citations in OpenAlex.
- Review
- DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly.Nature communications · 2026Article
- Polyadenylated versions of small non-coding RNAs inMicrobial cell (Graz, Austria) · 2024Article
- Tho2 is critical for the recruitment of Rrp6 to chromatin in response to perturbed mRNP biogenesis.RNA (New York, N.Y.) · 2023Article
- Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes.The Plant cell · 2022Review
- Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation.Nucleic acids research · 2022Article
- Substrate discrimination and quality control require each catalytic activity of TRAMP and the nuclear RNA exosome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Yeast RNA exosome activity is necessary for maintaining cell wall stability through proper protein glycosylation.Molecular biology of the cell · 2021Article
- From "Dark Matter" to "Star": Insight Into the Regulation Mechanisms of Plant Functional Long Non-Coding RNAs.Frontiers in plant science · 2021Review
- Rrp6 Moonlights in an RNA Exosome-Independent Manner to Promote Cell Survival and Gene Expression during Stress.Cell reports · 2020Article
- Substrate selectivity by the exonuclease Rrp6p.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The ribosome assembly factor Nop53 controls association of the RNA exosome with pre-60S particles in yeast.The Journal of biological chemistry · 2019Article
- Perturbation of mRNP biogenesis reveals a dynamic landscape of the Rrp6-dependent surveillance machinery trafficking along the yeast genome.RNA biology · 2019Article
- Stress-induced nuclear depletion ofThe Journal of biological chemistry · 2018Article
- Transcriptome-wide analysis of alternative routes for RNA substrates into the exosome complex.PLoS genetics · 2017Article
- The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome.Nucleic acids research · 2017Article
- Long Noncoding RNAs in Plants.Advances in experimental medicine and biology · 2017Review
- A conserved virus-induced cytoplasmic TRAMP-like complex recruits the exosome to target viral RNA for degradation.Genes & development · 2016Article
- Exosome Cofactors Connect Transcription Termination to RNA Processing by Guiding Terminated Transcripts to the Appropriate Exonuclease within the Nuclear Exosome.The Journal of biological chemistry · 2016Article
- Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RNA exosome processes and degrades RNAs in archaeal and eukaryotic cells. Exosomes from yeast and humans contain two active exoribonuclease components, Rrp6p and Dis3p/Rrp44p. Rrp6p is concentrated in the nucleus and the dependence of its function on the nine-subunit core exosome and Dis3p remains unclear. We found that cells lacking Rrp6p accumulate poly(A)+ rRNA degradation intermediates distinct from those found in cells depleted of Dis3p, or the core exosome component Rrp43p. Depletion of Dis3p in the absence of Rrp6p causes a synergistic increase in the levels of degradation substrates common to the core exosome and Rrp6p, but has no effect on Rrp6p-specific substrates. Rrp6p lacking a portion of its C-terminal domain no longer co-purifies with the core exosome, but continues to carry out RNA 3'-end processing of 5.8S rRNA and snoRNAs, as well as the degradation of certain truncated Rrp6-specific rRNA intermediates. However, disruption of Rrp6p-core exosome interaction results in the inability of the cell to efficiently degrade certain poly(A)+ rRNA processing products that require the combined activities of Dis3p and Rrp6p. These findings indicate that Rrp6p may carry out some of its critical functions without physical association with the core exosome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.