Evidence map›Paper›PMID 37604686›Full record

ArticleNucleic acids research2023

Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.

Ying-Hui Wang, Hong Dai, Ling Zhang, Yun Wu, Jingfen Wang, Chen Wang, Cai-Huang Xu, Hai Hou, Bing Yang, Yongqun Zhu and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Ying-Hui WangLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Hong DaiLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Ling ZhangLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Yun WuLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Jingfen WangCenter for Cryo-Electron Microscopy, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, China.
Chen WangCenter for Cryo-Electron Microscopy, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, China.
Cai-Huang XuCenter for Cryo-Electron Microscopy, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, China.
Hai HouInstitute of Medical Research, Northwestern Polytechnical University, Xi'an, Shaanxi 710072, China.
Bing YangLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.ORCID 0000-0001-6739-2932
Yongqun ZhuLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Xing ZhangCenter for Cryo-Electron Microscopy, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, China.
Jie ZhouLife Sciences Institute, Zhejiang University, Hangzhou, Zhejiang 310058, China.ORCID 0000-0001-6521-1384
Zhejiang University · CNSir Run Run Shaw Hospital · CNNorthwestern Polytechnical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Archaeal ribosomes have many domain-specific features; however, our understanding of these structures is limited. We present 10 cryo-electron microscopy (cryo-EM) structures of the archaeal ribosome from crenarchaeota Sulfolobus acidocaldarius (Sac) at 2.7-5.7 Å resolution. We observed unstable conformations of H68 and h44 of ribosomal RNA (rRNA) in the subunit structures, which may interfere with subunit association. These subunit structures provided models for 12 rRNA expansion segments and 3 novel r-proteins. Furthermore, the 50S-aRF1 complex structure showed the unique domain orientation of aRF1, possibly explaining P-site transfer RNA (tRNA) release after translation termination. Sac 70S complexes were captured in seven distinct steps of the tRNA translocation reaction, confirming conserved structural features during archaeal ribosome translocation. In aEF2-engaged 70S ribosome complexes, 3D classification of cryo-EM data based on 30S head domain identified two new translocation intermediates with 30S head domain tilted 5-6° enabling its disengagement from the translocated tRNA and its release post-translocation. Additionally, we observed conformational changes to aEF2 during ribosome binding and switching from three different states. Our structural and biochemical data provide new insights into archaeal translation and ribosome translocation.

Indexed as

RibosomesSulfolobus acidocaldariusCryoelectron MicroscopyRibosomal ProteinsRNA, RibosomalRNA, TransferRibosomal ProteinsRNA, RibosomalRNA, Transfer

Identifiers

PMID37604686
PMCPMC10516650
OpenAlexW4386023542

What OpenQuestion holds

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LicenceCC BY
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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.