Evidence map›Paper›PMID 27174052›Full record

ArticleCell research2016

CryoEM structure of yeast cytoplasmic exosome complex.

Jun-Jie Liu, Chu-Ya Niu, Yao Wu, Dan Tan, Yang Wang, Ming-Da Ye, Yang Liu, Wenwei Zhao, Ke Zhou, Quan-Sheng Liu and 5 more

Abstract read
In one paragraph

Article in Cell research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

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  9. Substrate discrimination and quality control require each catalytic activity of TRAMP and the nuclear RNA exosome.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  10. Review
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  15. Cryo-Electron Microscopy of Endogenous Yeast Exosomes.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  16. Article
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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

15 authors.

Jun-Jie LiuMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Chu-Ya NiuMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yao WuNational Institute of Biological Sciences, Beijing 102206, China.
Dan TanNational Institute of Biological Sciences, Beijing 102206, China.
Yang WangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Ming-Da YeMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yang LiuJoint Graduate Program of Peking-Tsinghua-National Institute of Biological Science, Tsinghua University, Beijing 100084, China.
Wenwei ZhaoMOE Key Laboratory of Bioinformatics, Tsinghua-Peking Joint Center for Life Sciences, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Ke ZhouThe Multidiscipline Research Center, Institute of High Energy Physics of the Chinese Academy of Sciences, Beijing 100049, China.
Quan-Sheng LiuThe Multidiscipline Research Center, Institute of High Energy Physics of the Chinese Academy of Sciences, Beijing 100049, China.
Junbiao DaiMOE Key Laboratory of Bioinformatics, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Xuerui YangMOE Key Laboratory of Bioinformatics, Tsinghua-Peking Joint Center for Life Sciences, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing 102206, China.
Niu HuangNational Institute of Biological Sciences, Beijing 102206, China.
Hong-Wei WangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic multi-subunit RNA exosome complex plays crucial roles in 3'-to-5' RNA processing and decay. Rrp6 and Ski7 are the major cofactors for the nuclear and cytoplasmic exosomes, respectively. In the cytoplasm, Ski7 helps the exosome to target mRNAs for degradation and turnover via a through-core pathway. However, the interaction between Ski7 and the exosome complex has remained unclear. The transaction of RNA substrates within the exosome is also elusive. In this work, we used single-particle cryo-electron microscopy to solve the structures of the Ski7-exosome complex in RNA-free and RNA-bound forms at resolutions of 4.2 Å and 5.8 Å, respectively. These structures reveal that the N-terminal domain of Ski7 adopts a structural arrangement and interacts with the exosome in a similar fashion to the C-terminal domain of nuclear Rrp6. Further structural analysis of exosomes with RNA substrates harboring 3' overhangs of different length suggests a switch mechanism of RNA-induced exosome activation in the through-core pathway of RNA processing.

Indexed as

Cryoelectron MicroscopyAdaptor Proteins, Signal TransducingAmino Acid SequenceExosome Multienzyme Ribonuclease ComplexExosomesImage Processing, Computer-AssistedModels, MolecularMutagenesisNucleic Acid ConformationProtein BindingProtein Structure, QuaternaryRNARNA-Binding MotifsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingExosome Multienzyme Ribonuclease ComplexRNARRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKI7 protein, S cerevisiae

Identifiers

PMID27174052
PMCPMC5129878

What OpenQuestion holds

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Registered trials

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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.