Evidence map›Paper›PMID 25319414›Full record

ArticleThe EMBO journal2014

The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.

Benjamin Schuch, Monika Feigenbutz, Debora L Makino, Sebastian Falk, Claire Basquin, Phil Mitchell, Elena Conti

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

79 citing papers in PubMed, 112 citations in OpenAlex.

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  6. TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025
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19 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Benjamin SchuchStructural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.
Monika FeigenbutzMolecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK.
Debora L MakinoStructural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.
Sebastian FalkStructural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.
Claire BasquinStructural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.
Phil MitchellMolecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de.
Elena ContiStructural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de.
Max Planck Institute of Biochemistry · DEUniversity of Sheffield · GB

Funding

Wellcome Trust 8836/Z/09/Z
6 · The paper itself

Abstract

The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and independently of other cofactors. Crystallographic analyses reveal that the N-terminal domains of Rrp6 and Rrp47 form a highly intertwined structural unit. Rrp6 and Rrp47 synergize to create a composite and conserved surface groove that binds the N-terminus of Mtr4. Mutation of conserved residues within Rrp6 and Mtr4 at the structural interface disrupts their interaction and inhibits growth of strains expressing a C-terminal GFP fusion of Mtr4. These studies provide detailed structural insight into the interaction between the Rrp6-Rrp47 complex and Mtr4, revealing an important link between Mtr4 and the core exosome.

Indexed as

Models, MolecularBlotting, WesternCalorimetryChromatography, GelCrystallizationDEAD-box RNA HelicasesDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliExosome Multienzyme Ribonuclease ComplexFluorescence PolarizationMultiprotein ComplexesNuclear ProteinsOligonucleotide ProbesProtein ConformationRNA-Binding ProteinsCoomassie blueDEAD-box RNA HelicasesDNA-Binding ProteinsExosome Multienzyme Ribonuclease ComplexLRP1 protein, S cerevisiaeMTR4 protein, S cerevisiaeMultiprotein ComplexesNuclear ProteinsOligonucleotide ProbesRNA-Binding ProteinsRosaniline DyesRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsnuclear exosomeRNA degradationX‐ray crystallographyyeast genetics

Identifiers

PMID25319414
PMCPMC4282559
OpenAlexW2075328195

What OpenQuestion holds

Textmetadata
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.