{"doi":"10.1128/jb.01961-14","title":"Acetyl Coenzyme A Synthetase Is Acetylated on Multiple Lysine Residues by a Protein Acetyltransferase with a Single Gcn5-Type\n            <i>N</i>\n            -Acetyltransferase (GNAT) Domain in Saccharopolyspora erythraea","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            Reversible lysine acetylation (RLA) is used by cells of all domains of life to modulate protein function. To date, bacterial acetylation/deacetylation systems have been studied in a few bacteria (e.g.,\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Salmonella enterica</jats:named-content>\n            ,\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus subtilis</jats:named-content>\n            ,\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli</jats:named-content>\n            ,\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Erwinia amylovora</jats:named-content>\n            ,\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Mycobacterium tuberculosis</jats:named-content>\n            , and\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Geobacillus kaustophilus</jats:named-content>\n            ), but little is known about RLA in antibiotic-producing actinomycetes. Here, we identify the Gcn5-like protein acetyltransferase AcuA of\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Saccharopolyspora erythraea</jats:named-content>\n            (\n            <jats:italic>Sac</jats:italic>\n            AcuA, SACE_5148) as the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase (\n            <jats:italic>Sac</jats:italic>\n            AcsA, SACE_2375). Acetylated\n            <jats:italic>Sac</jats:italic>\n            AcsA was deacetylated by a sirtuin-type NAD\n            <jats:sup>+</jats:sup>\n            -dependent consuming deacetylase (\n            <jats:italic>Sac</jats:italic>\n            SrtN, SACE_3798).\n            <jats:italic>In vitro</jats:italic>\n            acetylation/deacetylation of\n            <jats:italic>Sac</jats:italic>\n            AcsA enzyme was studied by Western blotting, and acetylation of lysine residues Lys\n            <jats:sup>237</jats:sup>\n            , Lys\n            <jats:sup>380</jats:sup>\n            , Lys\n            <jats:sup>611</jats:sup>\n            , and Lys\n            <jats:sup>628</jats:sup>\n            was confirmed by mass spectrometry. In a strain devoid of\n            <jats:italic>Sac</jats:italic>\n            AcuA, none of the above-mentioned Lys residues of\n            <jats:italic>Sac</jats:italic>\n            AcsA was acetylated. To our knowledge, the ability of\n            <jats:italic>Sac</jats:italic>\n            AcuA to acetylate multiple Lys residues is unique among AcuA-type acetyltransferases. Results from site-specific mutagenesis experiments showed that the activity of\n            <jats:italic>Sac</jats:italic>\n            AcsA was controlled by lysine acetylation. Lastly, immunoprecipitation data showed that\n            <jats:italic>in vivo</jats:italic>\n            acetylation of\n            <jats:italic>Sac</jats:italic>\n            AcsA was influenced by glucose and acetate availability. These results suggested that reversible acetylation may also be a conserved regulatory posttranslational modification strategy in antibiotic-producing actinomycetes.\n          </jats:p>","journal":"Journal of Bacteriology","year":2014,"id":14560,"datarank":1.2039774465914777,"base_score":3.8501476017100584,"endowment":3.8501476017100584,"self_citation_contribution":0.5775221402565088,"citation_network_contribution":0.6264553063349688,"self_endowment_contribution":0.5775221402565088,"citer_contribution":0.6264553063349688,"corpus_percentile":null,"corpus_rank":null,"citation_count":46,"citer_count":23,"citers_with_citation_signal":22,"citers_with_endowment":22,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":114500,"name":"Li-li Yao","orcid":null,"position":1,"is_corresponding":false},{"id":114501,"name":"Dan Huang","orcid":null,"position":2,"is_corresponding":false},{"id":114502,"name":"Jorge C. Escalante-Semerena","orcid":null,"position":3,"is_corresponding":false},{"id":114503,"name":"Bang-Ce Ye","orcid":"0000-0002-5555-5359","position":4,"is_corresponding":false},{"id":114499,"name":"Di You","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"citation_network_status":"fetched"},"created_at":"2026-06-01T12:06:13.608586Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}