Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae

Lactylation at lysine residue (Klac) modification is a novel PTM first discovered on histones in mammalian cells in 2019 [8]. It has been observed that Klac modification on histones modulates macrophage polarization and state, and influences cellular metabolic reprogramming in pluripotent stem cells and nonsmall cell lung cancer, and can even induce tumorigenesis [5,6]. Subsequent investigations have shown that Klac modification extends to non-histone proteins in various subcellular compartments and proteins in prokaryotic cells. To date, Klac modification has been extensively identified in various organisms, including humans [8,10-17], mice [18-20], rats [16], insects [21], plants (rice [22] and wheat [23]), fungi (Botrytis cinerea [24] and Phialophora verrucosa [25]), algae (Nannochloropsis oceanica [26]), parasites (Toxoplasma gondii [27] and Trypanosoma brucei [28]), and bacteria (Escherichia coli [5] and Streptococcus mutans [6]). These studies collectively demonstrate the evolutionary conservation of Klac modification across diverse organisms.