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

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.

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Publication Details

Journal
Nature Communications
Published
2025-08-14
DOI
https://doi.org/10.1038/s41467-025-62638-5
Citations
1
Primary Topic
Biochemical Acid Research Studies
Type
article
Field-Weighted Citation Impact
1.11

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article

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

Jiali Meng, An‐Ping Zeng, Zhijuan Hu, Minghua Kong et al.
1 citations
Nature Communications
Biochemical Acid Research Studies
1.11
article

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

Jiali Meng, An‐Ping Zeng, Zhijuan Hu, Minghua Kong, Yingying Wang, Zhe Zhang, Runqing Yang, Kun Shen
article en
1 citations

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.

Nature CommunicationsVol. 16(1)
Westlake University (CN)
Westlake University, National Natural Science Foundation of China, National Key Research and Development Program of China
Openalex Percentile: Top 20%
Biochemical Acid Research Studies
1.11
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