Evidence map›Paper›PMID 32855298›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress.

Ye Zhou, Panagiotis L Kastritis, Shannon E Dougherty, Jonathan Bouvette, Allen L Hsu, Laura Burbaum, Shyamal Mosalaganti, Stefan Pfeffer, Wim J H Hagen, Friedrich Förster and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

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  14. Ribosomes in RNA Granules Are Stalled on mRNA Sequences That Are Consensus Sites for FMRP Association.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
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  16. Quiescence inAnnual review of genetics · 2022
    Review
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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 at 7 institutions in 3 countries.

Ye ZhouDepartment of Computer Science, Duke University, Durham, NC 27708.ORCID 0000-0002-0489-3614
Panagiotis L KastritisInterdisciplinary Research Center HALOmem, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06120, Halle/Saale, Germany; panagiotis.kastritis@bct.uni-halle.de alberto.bartesaghi@duke.edu gustavo.silva@duke.edu.ORCID 0000-0002-1463-8422
Shannon E DoughertyDepartment of Biology, Duke University, Durham, NC 27708.
Jonathan BouvetteDepartment of Health and Human Services, Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Durham, NC 27709.
Allen L HsuDepartment of Health and Human Services, Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Durham, NC 27709.ORCID 0000-0003-2065-3802
Laura BurbaumDepartment of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Shyamal MosalagantiStructural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.ORCID 0000-0002-5934-687X
Stefan PfefferDepartment of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.ORCID 0000-0001-5843-2795
Wim J H HagenStructural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.ORCID 0000-0001-6229-2692
Friedrich FörsterDepartment of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Mario J BorgniaDepartment of Health and Human Services, Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Durham, NC 27709.ORCID 0000-0001-9159-1413
Christine VogelCenter for Genomics and Systems Biology, Department of Biology, New York University, New York, NY 10003.ORCID 0000-0002-2856-3118
Martin BeckStructural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
Alberto BartesaghiDepartment of Computer Science, Duke University, Durham, NC 27708; panagiotis.kastritis@bct.uni-halle.de alberto.bartesaghi@duke.edu gustavo.silva@duke.edu.ORCID 0000-0002-7360-1523
Gustavo M SilvaDepartment of Biology, Duke University, Durham, NC 27708; panagiotis.kastritis@bct.uni-halle.de alberto.bartesaghi@duke.edu gustavo.silva@duke.edu.ORCID 0000-0001-9476-069X
Duke University · USEuropean Molecular Biology Laboratory · DENational Institutes of Health · USMax Planck Institute of Biochemistry · DEMartin Luther University Halle-Wittenberg · DENew York University · USUtrecht University · NL

Funding

NIEHS Cryo-EM Core FacilityZICES103326 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BORGNIA, MARIO · 2017 to 2025
$17.0M
Next generation gene expression analysisR35GM127089 · NIGMS · NEW YORK UNIVERSITY · PI Christine Vogel · 2018 to 2026
$4.0M
Defining the roles of ubiquitination during the environmental stress responseR00ES025835 · NIEHS · DUKE UNIVERSITY · PI SILVA, GUSTAVO M · 2018 to 2020
$905k
Defining the roles of ubiquitination during the environmental stress responseK99ES025835 · NIEHS · NEW YORK UNIVERSITY · PI SILVA, GUSTAVO M · 2015 to 2016
$205k
Intramural NIH HHS ZIC ES103326NIEHS NIH HHS K99 ES025835NIEHS NIH HHS R00 ES025835NIGMS NIH HHS R35 GM127089
6 · The paper itself

Abstract

Subpopulations of ribosomes are responsible for fine tuning the control of protein synthesis in dynamic environments. K63 ubiquitination of ribosomes has emerged as a new posttranslational modification that regulates protein synthesis during cellular response to oxidative stress. K63 ubiquitin, a type of ubiquitin chain that functions independently of the proteasome, modifies several sites at the surface of the ribosome, however, we lack a molecular understanding on how this modification affects ribosome structure and function. Using cryoelectron microscopy (cryo-EM), we resolved the first three-dimensional (3D) structures of K63 ubiquitinated ribosomes from oxidatively stressed yeast cells at 3.5-3.2 Å resolution. We found that K63 ubiquitinated ribosomes are also present in a polysome arrangement, similar to that observed in yeast polysomes, which we determined using cryoelectron tomography (cryo-ET). We further showed that K63 ubiquitinated ribosomes are captured uniquely at the rotated pretranslocation stage of translation elongation. In contrast, cryo-EM structures of ribosomes from mutant cells lacking K63 ubiquitin resolved at 4.4-2.7 Å showed 80S ribosomes represented in multiple states of translation, suggesting that K63 ubiquitin regulates protein synthesis at a selective stage of elongation. Among the observed structural changes, ubiquitin mediates the destabilization of proteins in the 60S P-stalk and in the 40S beak, two binding regions of the eukaryotic elongation factor eEF2. These changes would impact eEF2 function, thus, inhibiting translocation. Our findings help uncover the molecular effects of K63 ubiquitination on ribosomes, providing a model of translation control during oxidative stress, which supports elongation halt at pretranslocation.

Indexed as

Oxidative StressCryoelectron MicroscopyGene Expression Regulation, FungalModels, MolecularMutationRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiae Proteinscryo-EMK63 ubiquitinoxidative stressribosometranslation

Identifiers

PMID32855298
PMCPMC7486741
OpenAlexW3080593232

What OpenQuestion holds

Textmetadata
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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.