ArticleNature2015
RNA degradation paths in a 12-subunit nuclear exosome complex.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 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
90 citing papers in PubMed, 136 citations in OpenAlex.
- Review
- Review
- 4D structural biology-quantitative dynamics in the eukaryotic RNA exosome complex.Nature communications · 2025Article
- Comparative analyses of disease-linked missense mutations in the RNA exosome modeled in budding yeast reveal distinct functional consequences in translation.RNA (New York, N.Y.) · 2025Article
- New insights into nuclear import and nucleolar localization of yeast RNA exosome subunits.Molecular biology of the cell · 2025Article
- Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Downregulation of the mThe Journal of biological chemistry · 2024Article
- A UTP3-dependent nucleolar translocation pathway facilitates pre-rRNA 5'ETS processing.Nucleic acids research · 2024Article
- Hypoxia-driven deSUMOylation of EXOSC10 promotes adaptive changes in the transcriptome profile.Cellular and molecular life sciences : CMLS · 2024Article
- Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions.Biochemistry · 2024Article
- Genome-Wide Characterization of the RNA Exosome Complex in Relation to Growth, Development, and Pathogenicity of Fusarium graminearum.Microbiology spectrum · 2023Article
- The ubiquitin-specific protease USP36 SUMOylates EXOSC10 and promotes the nucleolar RNA exosome function in rRNA processing.Nucleic acids research · 2023Article
- Review
- Dissecting Trypanosoma brucei RRP44 function in the maturation of segmented ribosomal RNA using a regulated genetic complementation system.Nucleic acids research · 2023Article
- Trypanosoma brucei RRP44: a versatile enzyme for processing structured and non-structured RNA substrates.Nucleic acids research · 2023Article
- MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus.Nucleic acids research · 2022Article
- Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome.Molecular cell · 2022Article
- Structural basis for RNA surveillance by the human nuclear exosome targeting (NEXT) complex.Cell · 2022Article
- Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site.Nucleic acids research · 2022Article
- Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation.Nucleic acids research · 2022Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic exosome is a conserved RNA-degrading complex that functions in RNA surveillance, turnover and processing. How the same machinery can either completely degrade or precisely trim RNA substrates has long remained unexplained. Here we report the crystal structures of a yeast nuclear exosome containing the 9-subunit core, the 3'-5' RNases Rrp44 and Rrp6, and the obligate Rrp6-binding partner Rrp47 in complex with different RNAs. The combined structural and biochemical data of this 12-subunit complex reveal how a single-stranded RNA can reach the Rrp44 or Rrp6 active sites directly or can bind Rrp6 and be threaded via the central channel towards the distal RNase Rrp44. When a bulky RNA is stalled at the entrance of the channel, Rrp6-Rrp47 swings open. The results suggest how the same molecular machine can coordinate processive degradation and partial trimming in an RNA-dependent manner by a concerted swinging mechanism of the two RNase subunits.
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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.