Evidence map›Paper›PMID 37737245›Full record

ArticleNature communications2023

Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex.

Xu Han, Dongliang Zhang, Lu Hong, Daqi Yu, Zhaolong Wu, Tian Yang, Michael Rust, Yuhai Tu, Qi Ouyang

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. The cyanobacterial circadian clock.Npj biological timing and sleep · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. The inner workings of an ancient biological clock.Trends in biochemical sciences · 2024
    Review
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

9 authors.

Xu HanState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.
Dongliang ZhangState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.
Lu HongGraduate Program in Biophysical Sciences, University of Chicago, Chicago, IL, 60637, USA.
Daqi YuState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.
Zhaolong WuState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.ORCID http://orcid.org/0000-0002-0537-6424
Tian YangState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.
Michael RustDepartments of Molecular Genetics and Cell Biology and of Physics, University of Chicago, Chicago, IL, 60637, USA. mrust@uchicago.edu.
Yuhai TuIBM T. J. Watson Research Center, Yorktown Heights, NY, 10598, USA. yuhai@us.ibm.com.ORCID http://orcid.org/0000-0002-4589-981X
Qi OuyangState Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China. qi@pku.edu.cn.

Funding

Molecular Mechanisms and Biochemical Circuits for Adaptation in Biological SystemsR35GM131734 · NIGMS · IBM THOMAS J. WATSON RESEARCH CENTER · PI TU, YUHAI · 2019 to 2024
$1.8M
Coupling between Circadian Rhythms and Metaboilsm in CyanobacteriaR01GM107369 · NIGMS · UNIVERSITY OF CHICAGO · PI RUST, MICHAEL · 2013 to 2017
$1.5M
The Biochemistry of Clock Function in Fluctuating EnvironmentsR01GM135382 · NIGMS · UNIVERSITY OF CHICAGO · PI RUST, MICHAEL · 2020 to 2023
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM107369NIGMS NIH HHS R01 GM135382NIGMS NIH HHS R35 GM131734
6 · The paper itself

Abstract

Biological processes are typically actuated by dynamic multi-subunit molecular complexes. However, interactions between subunits, which govern the functions of these complexes, are hard to measure directly. Here, we develop a general approach combining cryo-EM imaging technology and statistical modeling and apply it to study the hexameric clock protein KaiC in Cyanobacteria. By clustering millions of KaiC monomer images, we identify two major conformational states of KaiC monomers. We then classify the conformational states of (>160,000) KaiC hexamers by the thirteen distinct spatial arrangements of these two subunit states in the hexamer ring. We find that distributions of the thirteen hexamer conformational patterns for two KaiC phosphorylation mutants can be fitted quantitatively by an Ising model, which reveals a significant cooperativity between neighboring subunits with phosphorylation shifting the probability of subunit conformation. Our results show that a KaiC hexamer can respond in a switch-like manner to changes in its phosphorylation level.

Indexed as

Circadian ClocksCLOCK ProteinsCluster AnalysisCryoelectron MicroscopyModels, StatisticalCLOCK Proteins

Identifiers

PMID37737245
PMCPMC10516925

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.