Evidence map›Paper›PMID 40069234›Full record

ArticleNature communications2025

A globular protein exhibits rare phase behavior and forms chemically regulated orthogonal condensates in cells.

Jinglei Nie, Xinyi Zhang, Zhijuan Hu, Wei Wang, Martin A Schroer, Jie Ren, Dmitri Svergun, Anyang Chen, Peiguo Yang, An-Ping Zeng

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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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

10 authors.

Jinglei NieCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0009-0006-5950-6796
Xinyi ZhangCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China.
Zhijuan HuCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0009-0004-0571-0498
Wei WangInstitute of Bioprocess and Biosystems Engineering, Hamburg University of Technology, Hamburg, Germany.
Martin A SchroerNanoparticle Process Technology (NPPT), University of Duisburg-Essen, Duisburg, Germany.ORCID http://orcid.org/0000-0002-0747-3965
Jie RenState Key Laboratory for Biology of Plant Diseases and Insect Pests/Key Laboratory of Control of Biological Hazard Factors (Plant Origin) for Agri-product Quality and Safety, Ministry of Agriculture, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Dmitri SvergunEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation c/o DESY, Hamburg, Germany.
Anyang ChenCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0009-0001-8812-1688
Peiguo YangCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0002-2334-5664
An-Ping ZengCenter of Synthetic Biology and Integrated Bioengineering, Westlake University, Hangzhou, Zhejiang, China. zenganping@westlake.edu.cn.ORCID http://orcid.org/0000-0001-9768-7096

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins with chemically regulatable phase separation are of great interest in the fields of biomolecular condensates and synthetic biology. Intrinsically disordered proteins (IDPs) are the dominating building blocks of biomolecular condensates which often lack orthogonality and small-molecule regulation desired to create synthetic biomolecular condensates or membraneless organelles (MLOs). Here, we discover a well-folded globular protein, lipoate-protein ligase A (LplA) from E. coli involved in lipoylation of enzymes essential for one-carbon and energy metabolisms, that exhibits structural homomeric oligomerization and a rare LCST-type reversible phase separation in vitro. In both E. coli and human U2OS cells, LplA can form orthogonal condensates, which can be specifically dissolved by its natural substrate, the small molecule lipoic acid and its analogue lipoamide. The study of LplA phase behavior and its regulatability expands our understanding and toolkit of small-molecule regulatable protein phase behavior with impacts on biomedicine and synthetic biology.

Indexed as

Biomolecular CondensatesEscherichia coli ProteinsIntrinsically Disordered ProteinsEscherichia coliHumansLipoylationSynthetic BiologyThioctic AcidEscherichia coli ProteinsIntrinsically Disordered ProteinsThioctic Acid

Identifiers

PMID40069234
PMCPMC11897184

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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.