ArticleThe Journal of biological chemistry2011
The C-terminal region of the exosome-associated protein Rrp47 is specifically required for box C/D small nucleolar RNA 3'-maturation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 41 citations in OpenAlex.
- EXOSC3 S1-domain variants implicated in PCH1b alter RNA exosome cap subunit abundance and thermal stability disrupting rRNA processing and targeting of AU-rich mRNA.bioRxiv : the preprint server for biology · 2025Article
- Article
- Maturation of small nucleolar RNAs: from production to function.RNA biology · 2023Review
- The nucleolus is the site for inflammatory RNA decay during infection.Nature communications · 2022Article
- Contribution of domain structure to the function of the yeast DEDD family exoribonuclease and RNase T functional homolog, Rex1.RNA (New York, N.Y.) · 2022Article
- Landscape of functional interactions of human processive ribonucleases revealed by high-throughput siRNA screenings.iScience · 2021Article
- C/D box snoRNAs in viral infections: RNA viruses use old dogs for new tricks.Non-coding RNA research · 2019Review
- Stress-induced nuclear depletion ofThe Journal of biological chemistry · 2018Article
- Assembly of the small ribosomal subunit in yeast: mechanism and regulation.RNA (New York, N.Y.) · 2018Review
- Assembly and trafficking of box C/D and H/ACA snoRNPs.RNA biology · 2017Review
- C/D-box snoRNAs form methylating and non-methylating ribonucleoprotein complexes: Old dogs show new tricks.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Genes & development · 2017Review
- Dual Role of a SAS10/C1D Family Protein in Ribosomal RNA Gene Expression and Processing Is Essential for Reproduction in Arabidopsis thaliana.PLoS genetics · 2016Article
- C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response.Cell division · 2016Review
- Article
- The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.The EMBO journal · 2014Article
- The eukaryotic RNA exosome.Current opinion in structural biology · 2014Review
- Article
- Article
- Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6.RNA (New York, N.Y.) · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cells lacking the exosome-associated protein Rrp47 show similar defects in stable RNA processing to those observed in the absence of the catalytic subunit Rrp6, but the precise mechanism(s) by which Rrp47 functions together with Rrp6 remains unclear. Deletion complementation analyses defined an N-terminal region of Rrp47, largely coincident with the bioinformatically defined Sas10/C1D domain, which was sufficient for protein function in vivo. In vitro protein interaction studies demonstrated that this domain of Rrp47 binds the PMC2NT domain of Rrp6. Expression of the N-terminal domain of Rrp47 in yeast complemented most RNA-processing defects associated with the rrp47Δ mutant but failed to complement the defect observed in 3'-end maturation of box C/D small nucleolar RNAs. Consistent with these results, protein capture assays revealed an interaction between the C-terminal region of Rrp47 and the small nucleolar ribonucleoproteins Nop56 and Nop58. Filter binding assays demonstrated that deletion of the lysine-rich sequence at the C terminus of Rrp47 blocked RNA binding in vitro. Furthermore, a protein mutated both at the C terminus and within the N-terminal domain showed a synergistic defect in RNA binding without impacting on its ability to interact with Rrp6. These studies provide evidence for a role of Rrp47 in registering a small nucleolar ribonucleoprotein particle assembly, functionally characterize the Sas10/C1D domain of Rrp47, and show that both the C terminus of Rrp47 and the N-terminal domain contribute to its RNA-binding activity.
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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.