Evidence map›Paper›PMID 27251291›Full record

ArticleNature2016

Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes.

Shan Wu, Beril Tutuncuoglu, Kaige Yan, Hailey Brown, Yixiao Zhang, Dan Tan, Michael Gamalinda, Yi Yuan, Zhifei Li, Jelena Jakovljevic and 5 more

Abstract read
In one paragraph

Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
17.1field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 231 citations in OpenAlex.

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  12. Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025
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87 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

15 authors at 4 institutions in 2 countries.

Shan WuMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Beril TutuncuogluDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Kaige YanMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Hailey BrownDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Yixiao ZhangMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Dan TanGraduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China.
Michael GamalindaDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Yi YuanMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Zhifei LiMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jelena JakovljevicDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Chengying MaMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jianlin LeiMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Meng-Qiu DongGraduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China.
John L WoolfordDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Ning GaoMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Tsinghua University · CNCarnegie Mellon University · USChinese Academy of Medical Sciences & Peking Union Medical College · CNNational Institute of Biological Sciences, Beijing · CN

Funding

YEAST RIBOSOME BIOGENESISR01GM028301 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WOOLFORD, JOHN L. · 1985 to 2025
$8.4M
NIGMS NIH HHS R01 GM028301NIGMS NIH HHS R01GM028301
6 · The paper itself

Abstract

Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein) binding and ribosomal RNA remodelling events in the nucleolus, nucleoplasm and cytoplasm. Hundreds of assembly factors, organized into sequential functional groups, facilitate and guide the maturation process into productive assembly branches in and across different cellular compartments. However, the precise mechanisms by which these assembly factors function are largely unknown. Here we use cryo-electron microscopy to characterize the structures of yeast nucleoplasmic pre-60S particles affinity-purified using the epitope-tagged assembly factor Nog2. Our data pinpoint the locations and determine the structures of over 20 assembly factors, which are enriched in two areas: an arc region extending from the central protuberance to the polypeptide tunnel exit, and the domain including the internal transcribed spacer 2 (ITS2) that separates 5.8S and 25S ribosomal RNAs. In particular, two regulatory GTPases, Nog2 and Nog1, act as hub proteins to interact with multiple, distant assembly factors and functional ribosomal RNA elements, manifesting their critical roles in structural remodelling checkpoints and nuclear export. Moreover, our snapshots of compositionally and structurally different pre-60S intermediates provide essential mechanistic details for three major remodelling events before nuclear export: rotation of the 5S ribonucleoprotein, construction of the active centre and ITS2 removal. The rich structural information in our structures provides a framework to dissect molecular roles of diverse assembly factors in eukaryotic ribosome assembly.

Indexed as

Cryoelectron MicroscopyActive Transport, Cell NucleusBase SequenceCatalytic DomainCell NucleusCytoplasmDNA, Ribosomal SpacerGTP-Binding ProteinsGTP PhosphohydrolasesModels, MolecularMolecular Sequence DataNuclear ProteinsProtein BindingRibonucleoproteinsRibosomal ProteinsRibosome Subunits, Large, EukaryoticDNA, Ribosomal SpacerGTP-Binding ProteinsGTP PhosphohydrolasesNOG1 protein, S cerevisiaeNOG2 protein, S cerevisiaeNuclear ProteinsRibonucleoproteinsRibosomal ProteinsRNA, FungalRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID27251291
PMCPMC5237361
OpenAlexW2407366427

What OpenQuestion holds

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LicenceTDM
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.