Evidence map›Paper›PMID 33037216›Full record

ArticleNature communications2020

Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel.

Daniel M Wilson, Yu Li, Amber LaPeruta, Michael Gamalinda, Ning Gao, John L Woolford

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Impacts of ribosomal RNA sequence variation on gene expression and phenotype.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Article
  8. Review
  9. Article
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  11. Article
  12. Review
  13. Article
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  16. Article
  17. Article
  18. 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

6 authors.

Daniel M Wilson *Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Yu Li *State Key Laboratory of Membrane Biology, School of Life Science, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-4844-3359
Amber LaPerutaDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Michael GamalindaDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
Ning GaoState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China. gaon@pku.edu.cn.ORCID http://orcid.org/0000-0003-3067-9993
John L WoolfordDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA. jw17@andrew.cmu.edu.ORCID http://orcid.org/0000-0002-7553-7043

Funding

YEAST RIBOSOME BIOGENESISR01GM028301 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WOOLFORD, JOHN L. · 1985 to 2025
$8.4M
NIGMS NIH HHS R01 GM028301
6 · The paper itself

Abstract

The nascent polypeptide exit tunnel (NPET) is a major functional center of 60S ribosomal subunits. However, little is known about how the NPET is constructed during ribosome assembly. We utilized molecular genetics, biochemistry, and cryo-electron microscopy (cryo-EM) to investigate the functions of two NPET-associated proteins, ribosomal protein uL4 and assembly factor Nog1, in NPET assembly. Structures of mutant pre-ribosomes lacking the tunnel domain of uL4 reveal a misassembled NPET, including an aberrantly flexible ribosomal RNA helix 74, resulting in at least three different blocks in 60S assembly. Structures of pre-ribosomes lacking the C-terminal extension of Nog1 demonstrate that this extension scaffolds the tunnel domain of uL4 in the NPET to help maintain stability in the core of pre-60S subunits. Our data reveal that uL4 and Nog1 work together in the maturation of ribosomal RNA helix 74, which is required to ensure proper construction of the NPET and 60S ribosomal subunits.

Indexed as

Cell Cycle ProteinsCryoelectron MicroscopyGTP-Binding ProteinsModels, MolecularMutationNuclear ProteinsProtein DomainsRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA, RibosomalRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsGTP-Binding ProteinsNOG1 protein, S cerevisiaeNuclear Proteinsribosomal protein L4Ribosomal ProteinsRNA, RibosomalSaccharomyces cerevisiae ProteinsSDA1 protein, S cerevisiae

Identifiers

PMID33037216
PMCPMC7547690

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.