Evidence map›Paper›PMID 27899565›Full record

ArticleNucleic acids research2017

The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome.

Elizabeth V Wasmuth, Christopher D Lima

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 53 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Elizabeth V WasmuthStructural Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA.
Christopher D LimaStructural Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA limac@mskcc.org.
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Structural studies of RNA processing and ubiquitin-like protein modificationR35GM118080 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI CHRISTOPHER D. LIMA · 2016 to 2026
$5.0M
Structural and Functional Studies of Eukaryotic ExosomesR01GM079196 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LIMA, CHRISTOPHER D. · 2008 to 2015
$2.5M
Structural and Biochemical Characterization of the S. cerevisiae RNA ExosomeF31GM097910 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI WASMUTH, ELIZABETH VICTORINA · 2011 to 2014
$169k
NCI NIH HHS P30 CA008748NIGMS NIH HHS F31 GM097910NIGMS NIH HHS R01 GM079196NIGMS NIH HHS R35 GM118080
6 · The paper itself

Abstract

The eukaryotic RNA exosome is an essential, multi-subunit complex that catalyzes RNA turnover, maturation, and quality control processes. Its non-catalytic donut-shaped core includes 9 subunits that associate with the 3' to 5' exoribonucleases Rrp6, and Rrp44/Dis3, a subunit that also catalyzes endoribonuclease activity. Although recent structures and biochemical studies of RNA bound exosomes from S. cerevisiae revealed that the Exo9 central channel guides RNA to either Rrp6 or Rrp44 using partially overlapping and mutually exclusive paths, several issues related to RNA recruitment remain. Here, we identify activities for the highly basic Rrp6 C-terminal tail that we term the 'lasso' because it binds RNA and stimulates ribonuclease activities associated with Rrp44 and Rrp6 within the 11-subunit nuclear exosome. Stimulation is dependent on the Exo9 central channel, and the lasso contributes to degradation and processing activities of exosome substrates in vitro and in vivo. Finally, we present evidence that the Rrp6 lasso may be a conserved feature of the eukaryotic RNA exosome.

Indexed as

Protein Interaction Domains and MotifsExoribonucleasesExosome Multienzyme Ribonuclease ComplexHumansModels, MolecularMolecular ConformationMutationProtein BindingRNARNA StabilityDIS3 protein, humanExoribonucleasesEXOSC10 protein, humanExosome Multienzyme Ribonuclease ComplexRNA

Identifiers

PMID27899565
PMCPMC5314766
OpenAlexW2557470621

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.