Lysine acetylation regulates the AT-rich DNA possession ability of H-NS.

Yabo Liu, Mengqing Zhou, Yifan Bu, Liang Qin, Yuanxing Zhang, Shuai Shao, Qiyao Wang

Nucleic acids research 2024 Feb 28

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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. © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

Citation

Yabo Liu, Mengqing Zhou, Yifan Bu, Liang Qin, Yuanxing Zhang, Shuai Shao, Qiyao Wang. Lysine acetylation regulates the AT-rich DNA possession ability of H-NS. Nucleic acids research. 2024 Feb 28;52(4):1645-1660