{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu Y"],"funding":["China Agriculture Research System of MOF and MARA","National Natural Science Foundation of China"],"pagination":["1645-1660"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10899749"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(4)"],"pubmed_abstract":["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"],"journal":["Nucleic acids research"],"pubmed_title":["Lysine acetylation regulates the AT-rich DNA possession ability of H-NS."],"pmcid":["PMC10899749"],"funding_grant_id":["CARS-47","32002436","32130108"],"pubmed_authors":["Zhou M","Liu Y","Bu Y","Qin L","Wang Q","Zhang Y","Shao S"],"additional_accession":[]},"is_claimable":false,"name":"Lysine acetylation regulates the AT-rich DNA possession ability of H-NS.","description":"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","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2025-05-18T12:53:33.76Z","creation":"2025-05-18T12:53:33.76Z"},"accession":"S-EPMC10899749","cross_references":{"pubmed":["38059366"],"doi":["10.1093/nar/gkad1172"]}}