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 and An-Ping Zeng ()
Additional contact information
Runqing Yang: Westlake University
Yingying Wang: Westlake University
Minghua Kong: Westlake University
Zhijuan Hu: Westlake University
Zhe Zhang: Westlake University
Kun Shen: Westlake University
Jiali Meng: Westlake University
An-Ping Zeng: Westlake University

Nature Communications, 2025, vol. 16, issue 1, 1-21

Abstract: 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.

Date: 2025
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-62638-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62638-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-62638-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().