Evidence map›Paper›PMID 40813772›Full record

ArticleNature communications2025

Boosting energy metabolism and biosynthesis in diverse organisms by a common bacterial salvage lipoylation protein.

Runqing Yang, Yingying Wang, Minghua Kong, Zhijuan Hu, Zhe Zhang, Kun Shen, Jiali Meng, 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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

8 authors.

Runqing Yang *School of Engineering, Westlake University, Hangzhou, Zhejiang, China.
Yingying Wang *School of Engineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0002-0603-6691
Minghua Kong *School of Engineering, Westlake University, Hangzhou, Zhejiang, China.
Zhijuan HuSchool of Engineering, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0009-0004-0571-0498
Zhe ZhangSchool of Engineering, Westlake University, Hangzhou, Zhejiang, China.
Kun ShenSchool of Engineering, Westlake University, Hangzhou, Zhejiang, China.
Jiali MengSchool of Engineering, Westlake University, Hangzhou, Zhejiang, China.
An-Ping ZengSchool of Engineering, Westlake University, Hangzhou, Zhejiang, China. zenganping@westlake.edu.cn.ORCID http://orcid.org/0000-0001-9768-7096

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32200310
6 · The paper itself

Abstract

Lipoylation is a highly conserved post-translational modification (PTM) crucial for energy metabolism enzymes, with distinct pathways across organisms. Whereas bacteria like Escherichia coli inherit both salvage and de novo pathways, only the latter is found in eukaryotes. Here, we present a PTM-based strategy that achieves multiple metabolic benefits with a single intervention. By expressing E. coli-derived lipoate protein ligase A (LplA) from the salvage pathway, we enhance lipoylation and the activities of the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase complexes and glycine cleavage system in mammalian, algal and fungal cells, leading to improved energy metabolism, cofactor supply, mitochondrial function, and overall cell physiology. Our approach specifically targets multiple metabolic hubs through PTM modulation. Beyond its fundamental significance, our finding presents a unified and efficient way to boost biosynthesis across organisms, demonstrated in antibody production in Chinese hamster ovary cells, fatty acids synthesis in cyanobacteria and diatoms, and organic acid production in fungi.

Indexed as

Energy MetabolismEscherichia coliEscherichia coli ProteinsLipoylationPeptide SynthasesAnimalsCHO CellsCricetulusDiatomsFatty AcidsHumansKetoglutarate Dehydrogenase ComplexProtein Processing, Post-TranslationalPyruvate Dehydrogenase ComplexEscherichia coli ProteinsFatty AcidsKetoglutarate Dehydrogenase Complexlipoate-protein ligasePeptide SynthasesPyruvate Dehydrogenase Complex

Identifiers

PMID40813772
PMCPMC12354856

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.