Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella
Lysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins i...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2025-12-01
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| Series: | Emerging Microbes and Infections |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/22221751.2025.2475838 |
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| author | Chuanzhen Zhang Tao Zhou Chengxi Li Danni Wang Jing Tao Xiaocen Zhu Jie Lu Jinjing Ni Yu-Feng Yao |
| author_facet | Chuanzhen Zhang Tao Zhou Chengxi Li Danni Wang Jing Tao Xiaocen Zhu Jie Lu Jinjing Ni Yu-Feng Yao |
| author_sort | Chuanzhen Zhang |
| collection | DOAJ |
| description | Lysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins involved in metabolic processes, protein translation, and other biological functions are lactylated, with lactylation levels varying according to the growth phase or lactate supplementation. Lactylation is regulated by glycolysis, and inhibition of L-lactate utilization can enhance lactylation levels. In addition to the known lactylase in E. coli, the acetyltransferase YfiQ can also catalyse lactylation. More importantly, L-lactyl coenzyme A (L-La-CoA) and S,D-lactoylglutathione (LGSH) can directly donate lactyl groups to target proteins for chemical lactylation. Lactylation is involved in Salmonella invasion of eukaryotic cells, suggesting that lactylation is crucial for bacterial virulence. Collectively, we have comprehensively investigated protein lactylome and the regulatory mechanisms of lactylation in Salmonella, providing valuable insights into studying lactylation function across diverse bacterial species. |
| format | Article |
| id | doaj-art-d12d68f7256f4bfdbd3f1008532f0dbc |
| institution | Kabale University |
| issn | 2222-1751 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Emerging Microbes and Infections |
| spelling | doaj-art-d12d68f7256f4bfdbd3f1008532f0dbc2025-08-20T03:48:28ZengTaylor & Francis GroupEmerging Microbes and Infections2222-17512025-12-0114110.1080/22221751.2025.2475838Deciphering novel enzymatic and non-enzymatic lysine lactylation in SalmonellaChuanzhen Zhang0Tao Zhou1Chengxi Li2Danni Wang3Jing Tao4Xiaocen Zhu5Jie Lu6Jinjing Ni7Yu-Feng Yao8Laboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaLaboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaAnhui Key Laboratory of Infection and Immunity, Department of Microbiology, Bengbu Medical College, Bengbu, People’s Republic of ChinaLaboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaLaboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaCore Facility of Basic Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaDepartment of Infectious Diseases, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaLaboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaLaboratory of Bacterial Pathogenesis, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, People’s Republic of ChinaLysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins involved in metabolic processes, protein translation, and other biological functions are lactylated, with lactylation levels varying according to the growth phase or lactate supplementation. Lactylation is regulated by glycolysis, and inhibition of L-lactate utilization can enhance lactylation levels. In addition to the known lactylase in E. coli, the acetyltransferase YfiQ can also catalyse lactylation. More importantly, L-lactyl coenzyme A (L-La-CoA) and S,D-lactoylglutathione (LGSH) can directly donate lactyl groups to target proteins for chemical lactylation. Lactylation is involved in Salmonella invasion of eukaryotic cells, suggesting that lactylation is crucial for bacterial virulence. Collectively, we have comprehensively investigated protein lactylome and the regulatory mechanisms of lactylation in Salmonella, providing valuable insights into studying lactylation function across diverse bacterial species.https://www.tandfonline.com/doi/10.1080/22221751.2025.2475838SalmonellalactylationL-La-CoALGSHvirulence |
| spellingShingle | Chuanzhen Zhang Tao Zhou Chengxi Li Danni Wang Jing Tao Xiaocen Zhu Jie Lu Jinjing Ni Yu-Feng Yao Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella Emerging Microbes and Infections Salmonella lactylation L-La-CoA LGSH virulence |
| title | Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella |
| title_full | Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella |
| title_fullStr | Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella |
| title_full_unstemmed | Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella |
| title_short | Deciphering novel enzymatic and non-enzymatic lysine lactylation in Salmonella |
| title_sort | deciphering novel enzymatic and non enzymatic lysine lactylation in salmonella |
| topic | Salmonella lactylation L-La-CoA LGSH virulence |
| url | https://www.tandfonline.com/doi/10.1080/22221751.2025.2475838 |
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