ArticleThe Journal of biological chemistry2013
Assembly of the yeast exoribonuclease Rrp6 with its associated cofactor Rrp47 occurs in the nucleus and is critical for the controlled expression of Rrp47.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus.Nucleic acids research · 2022Article
- Rrp6 Moonlights in an RNA Exosome-Independent Manner to Promote Cell Survival and Gene Expression during Stress.Cell reports · 2020Article
- Reconstitution of the Human Nuclear RNA Exosome.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Reconstitution of the Schizosaccharomyces pombe RNA Exosome.Methods in molecular biology (Clifton, N.J.) · 2020Article
- RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020Review
- Perturbation of mRNP biogenesis reveals a dynamic landscape of the Rrp6-dependent surveillance machinery trafficking along the yeast genome.RNA biology · 2019Article
- Precise Post-translational Tuning Occurs for Most Protein Complex Components during Meiosis.Cell reports · 2018Article
- Stress-induced nuclear depletion ofThe Journal of biological chemistry · 2018Article
- Article
- Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 inThe Journal of biological chemistry · 2017Article
- The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome.Nucleic acids research · 2017Article
- C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response.Cell division · 2016Review
- A strategy for dissecting the architectures of native macromolecular assemblies.Nature methods · 2015Article
- Review
- The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.The EMBO journal · 2014Article
- 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
- Cotranscriptional recruitment of RNA exosome cofactors Rrp47p and Mpp6p and two distinct Trf-Air-Mtr4 polyadenylation (TRAMP) complexes assists the exonuclease Rrp6p in the targeting and degradation of an aberrant messenger ribonucleoprotein particle (mRNP) in yeast.The Journal of biological chemistry · 2013Article
- Article
- Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Rrp6 is a key catalytic subunit of the nuclear RNA exosome that plays a pivotal role in the processing, degradation, and quality control of a wide range of cellular RNAs. Here we report our findings on the assembly of the complex involving Rrp6 and its associated protein Rrp47, which is required for many Rrp6-mediated RNA processes. Recombinant Rrp47 is expressed as a non-globular homodimer. Analysis of the purified recombinant Rrp6·Rrp47 complex revealed a heterodimer, suggesting that Rrp47 undergoes a structural reconfiguration upon interaction with Rrp6. Studies using GFP fusion proteins show that Rrp6 and Rrp47 are localized to the yeast cell nucleus independently of one another. Consistent with this data, Rrp6, but not Rrp47, is found associated with the nuclear import adaptor protein Srp1. We show that the interaction with Rrp6 is critical for Rrp47 stability in vivo; in the absence of Rrp6, newly synthesized Rrp47 is rapidly degraded in a proteasome-dependent manner. These data resolve independent nuclear import routes for Rrp6 and Rrp47, reveal a structural reorganization of Rrp47 upon its interaction with Rrp6, and demonstrate a proteasome-dependent mechanism that efficiently suppresses the expression of Rrp47 in the absence of Rrp6.
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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.