{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Junyu Xu"],"species":["Mycolicibacterium Smegmatis Mc2 51"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0015202000"],"submitter_email":["jyxu@simm.ac.cn"],"submitter_affiliation":["Chinese Academy of Sciences Shanghai Institute of Materia Medica"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Lysine Acetylation of Translation Initiation Factor IF-2 Mediated by Mycobacterial Acetyltransferase Eis","description":"In our study, we employed the non-pathogenic Mycobacterium smegmatis as a model organism and applied a multi-omics approach to elucidate the substrate specificity and regulatory function of the mycobacterial acetyltransferase Eis. Through the integration of TMT-based acetyl-proteomics, dimethyl labeling-based acetyl-proteomics, and protein interactome analyses, we identified lysine 509 of the translation initiation factor IF-2 (infB), which is involved in ribosomal function, as a novel substrate of Eis. Acetylation at K509 was found to inhibit the GTPase activity of infB, leading to a decrease in the biosynthesis of nascent proteins. Furthermore, we demonstrated that Eis-mediated acetylation of infB reduced the tolerance of bioengineered M. smegmatis strain to the ribosome-targeting antibiotic clarithromycin and increased the production of inflammatory cytokines infected in the macrophage THP-1 cell line and mouse kidney. Our findings elucidate the Eis-infB regulatory axis, highlighting the critical roles of infB K509 acetylation in modulating mycobacterial homeostasis, ribosomal function, and host immune responses.","dates":{"publication":"Fri Apr 10 00:00:00 BST 2026"},"accession":"PXD076847","cross_references":{"TAXONOMY":["1445611"]}}