文献类型：期刊文献

英文题名：Lysine acetylation regulates the AT-rich DNA possession ability of H-NS

作者：Liu, Yabo[1];Zhou, Mengqing[1];Bu, Yifan[1];Qin, Liang[3];Zhang, Yuanxing[2,4,5];Shao, Shuai[1,4,5];Wang, Qiyao[1,2,4,5]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Qingdao Natl Lab Marine Sci & Technol, Lab Marine Fisheries Sci & Food Prod Proc, Qingdao, Peoples R China;[3]GenScript Biotech Corp, New Prod R&D, Nanjing 211100, Peoples R China;[4]Shanghai Engn Res Ctr Maricultured Anim Vaccines, Shanghai 200237, Peoples R China;[5]Lab Aquat Anim Dis MOA, Shanghai 200237, Peoples R China

年份：2024

卷号：52

期号：4

起止页码：1645

外文期刊名：NUCLEIC ACIDS RESEARCH

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001114736300001)】；

基金：National Natural Science Foundation of China [32130108, 32002436]; China Agriculture Research System of MOF and MARA [CARS-47]. Funding for open access charge: National Natural Science Foundation of China [32130108].

语种：英文

摘要：H-NS, the histone-like nucleoid-structuring protein in bacteria, regulates the stability of the bacterial genome by inhibiting the transcription of horizontally transferred genes, such as the type III and type VI secretion systems (T3/T6SS). While eukaryotic histone posttranslational modifications (PTMs) have been extensively studied, little is known about prokaryotic H-NS PTMs. Here, we report that the acetylation of H-NS attenuates its ability to silence horizontally transferred genes in response to amino acid nutrition and immune metabolites. Moreover, LC-MS/MS profiling showed that the acetyllysine sites of H-NS and K120 are indispensable for its DNA-binding ability. Acetylation of K120 leads to a low binding affinity for DNA and enhances T3/T6SS expression. Furthermore, acetylation of K120 impairs the AT-rich DNA recognition ability of H-NS. In addition, lysine acetylation in H-NS modulates in vivo bacterial virulence. These findings reveal the mechanism underlying H-NS PTMs and propose a novel mechanism by which bacteria counteract the xenogeneic silencing of H-NS. Graphical Abstract