Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae
Lysine lactylation (Klac) is a recently discovered post-translational modification (PTM) widespread across species, playing a crucial role in cellular processes and associated with pathological conditions. Photobacterium damselae subsp. damselae, a marine bacterium within the Vibrionaceae family, is...
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Frontiers Media S.A.
2025-06-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2025.1539893/full |
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| author | Yongxiang Yu Yongxiang Yu Haozhe Liu Chunyuan Wang Yingeng Wang Yingeng Wang Xiaojun Rong Xiaojun Rong Meijie Liao Meijie Liao Bin Li Bin Li Xingling Yi Zheng Zhang Zheng Zhang |
| author_facet | Yongxiang Yu Yongxiang Yu Haozhe Liu Chunyuan Wang Yingeng Wang Yingeng Wang Xiaojun Rong Xiaojun Rong Meijie Liao Meijie Liao Bin Li Bin Li Xingling Yi Zheng Zhang Zheng Zhang |
| author_sort | Yongxiang Yu |
| collection | DOAJ |
| description | Lysine lactylation (Klac) is a recently discovered post-translational modification (PTM) widespread across species, playing a crucial role in cellular processes and associated with pathological conditions. Photobacterium damselae subsp. damselae, a marine bacterium within the Vibrionaceae family, is a notable pathogen in aquaculture, offering a valuable model for investigating the evolution of pathogenicity from environmental ancestors and assessing the impact of genetic diversity-generating mechanisms on bacterial populations. Therefore, we conducted the first systematic analysis of Klac modification in P. damselae using highly sensitive proteomic techniques. A total of 1,352 Klac modification sites were identified on 486 proteins. The analysis of GO annotations and KEGG pathways for the identified Klac-modified proteins revealed their widespread distribution in subcellular compartments, indicating their involvement in diverse cellular functions and metabolic pathways, particularly in ribosome and protein biosynthesis, as well as central carbon metabolism. Furthermore, 20 highly connected Klac protein clusters were extracted from the global protein-protein interaction (PPI) network, indicating that Klac modification tends to occur on proteins associated with specific functional clusters. These findings enhance our understanding of the functional role of Klac modification and provide a dataset for further exploration of its impact on the physiology and biology of P. damselae. |
| format | Article |
| id | doaj-art-912d0cce1bb44e17adb5f8c2db2bdd66 |
| institution | DOAJ |
| issn | 1664-302X |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj-art-912d0cce1bb44e17adb5f8c2db2bdd662025-08-20T02:39:29ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2025-06-011610.3389/fmicb.2025.15398931539893Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselaeYongxiang Yu0Yongxiang Yu1Haozhe Liu2Chunyuan Wang3Yingeng Wang4Yingeng Wang5Xiaojun Rong6Xiaojun Rong7Meijie Liao8Meijie Liao9Bin Li10Bin Li11Xingling Yi12Zheng Zhang13Zheng Zhang14State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaWeimi Biotechnology Co., Ltd., Hangzhou, Zhejiang, ChinaState Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, ChinaLaboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, ChinaLysine lactylation (Klac) is a recently discovered post-translational modification (PTM) widespread across species, playing a crucial role in cellular processes and associated with pathological conditions. Photobacterium damselae subsp. damselae, a marine bacterium within the Vibrionaceae family, is a notable pathogen in aquaculture, offering a valuable model for investigating the evolution of pathogenicity from environmental ancestors and assessing the impact of genetic diversity-generating mechanisms on bacterial populations. Therefore, we conducted the first systematic analysis of Klac modification in P. damselae using highly sensitive proteomic techniques. A total of 1,352 Klac modification sites were identified on 486 proteins. The analysis of GO annotations and KEGG pathways for the identified Klac-modified proteins revealed their widespread distribution in subcellular compartments, indicating their involvement in diverse cellular functions and metabolic pathways, particularly in ribosome and protein biosynthesis, as well as central carbon metabolism. Furthermore, 20 highly connected Klac protein clusters were extracted from the global protein-protein interaction (PPI) network, indicating that Klac modification tends to occur on proteins associated with specific functional clusters. These findings enhance our understanding of the functional role of Klac modification and provide a dataset for further exploration of its impact on the physiology and biology of P. damselae.https://www.frontiersin.org/articles/10.3389/fmicb.2025.1539893/fullPhotobacterium damselae subsp. damselaepost-translational modification (PTM)lysine lactylation (Klac)proteomicsprotein-protein interaction (PPI) network |
| spellingShingle | Yongxiang Yu Yongxiang Yu Haozhe Liu Chunyuan Wang Yingeng Wang Yingeng Wang Xiaojun Rong Xiaojun Rong Meijie Liao Meijie Liao Bin Li Bin Li Xingling Yi Zheng Zhang Zheng Zhang Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae Frontiers in Microbiology Photobacterium damselae subsp. damselae post-translational modification (PTM) lysine lactylation (Klac) proteomics protein-protein interaction (PPI) network |
| title | Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae |
| title_full | Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae |
| title_fullStr | Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae |
| title_full_unstemmed | Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae |
| title_short | Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae |
| title_sort | global analysis of protein lysine lactylation profiles in the marine bacterium photobacterium damselae subsp damselae |
| topic | Photobacterium damselae subsp. damselae post-translational modification (PTM) lysine lactylation (Klac) proteomics protein-protein interaction (PPI) network |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2025.1539893/full |
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