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Genetic and biochemical studies on the LT2 type strain of\n                      <jats:italic toggle=\"yes\">Salmonella enterica<\/jats:italic>\n                      serovar Typhimurium determined the need for RidA to prevent metabolic stress caused by 2-aminoacrylate (2AA). RidA is an enamine deaminase, and in its absence, 2AA accumulates and can irreversibly damage critical pyridoxal 5\u2032-phosphate-dependent enzymes. Unexpectedly, the disruption of\n                      <jats:italic toggle=\"yes\">ridA<\/jats:italic>\n                      in a virulent type strain (\n                      <jats:italic toggle=\"yes\">S. enterica<\/jats:italic>\n                      serovar Typhimurium strain 14028s) did not replicate the serine sensitivity observed in LT2. Consistent with reported differences between these strains, the status of\n                      <jats:italic toggle=\"yes\">rpoS<\/jats:italic>\n                      impacted the phenotypes caused by a\n                      <jats:italic toggle=\"yes\">ridA<\/jats:italic>\n                      mutation. Specifically, serine sensitivity in the 14028s strain background occurred only when an insertion in\n                      <jats:italic toggle=\"yes\">rpoS<\/jats:italic>\n                      was combined with a mutation in\n                      <jats:italic toggle=\"yes\">ridA<\/jats:italic>\n                      . Further data suggest the 14028s\n                      <jats:italic toggle=\"yes\">rpoS ridA<\/jats:italic>\n                      growth deficiency is due to poor expression of\n                      <jats:italic toggle=\"yes\">sdaA<\/jats:italic>\n                      , which encodes an Fe-S cluster serine deaminase. Additional combinatorial effects of lesions in\n                      <jats:italic toggle=\"yes\">ridA<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">rpoS<\/jats:italic>\n                      indicate that the functional status of RpoS modulates the metabolic network in multiple ways that impact the cellular response to 2AA.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        RidA is an enamine\/imine deaminase known for mediating 2-aminoacrylate (2AA)-induced stress in several bacterial models. Best characterized in\n                        <jats:italic toggle=\"yes\">S. enterica<\/jats:italic>\n                        , manipulations to RidA have been used to probe metabolic flux in various bacteria. Here, we find that a key factor in the manifestation of 2AA stress is the status of transcriptional regulator RpoS. Our results indicate that a functional RpoS mediates some of the stress induced by exogenous serine in a\n                        <jats:italic toggle=\"yes\">ridA<\/jats:italic>\n                        mutant strain and further implicates this regulator in modulating the metabolic network. These results bolster our understanding of the flux and robustness integral to bacterial metabolism and emphasize a need to better understand the involvement of the RpoS regulon.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00390-26","type":"journal-article","created":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T13:46:12Z","timestamp":1789739172000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["The status of RpoS impacts the 2-aminoacrylate stress paradigm in\n                    <i>ridA<\/i>\n                    mutants of\n                    <i>Salmonella enterica<\/i>\n                    serovar Typhimurium"],"prefix":"10.1128","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-6703-6010","authenticated-orcid":false,"given":"Andrea","family":"Giuliano","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02bjhwk41","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology, University of Georgia","place":["Athens, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8165-7471","authenticated-orcid":true,"given":"Jessica K.","family":"Novak","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02bjhwk41","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology, University of Georgia","place":["Athens, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1564-6205","authenticated-orcid":true,"given":"Diana M.","family":"Downs","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02bjhwk41","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology, University of Georgia","place":["Athens, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","published-online":{"date-parts":[[2026,9,18]]},"reference":[{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.60.080805.142308"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/gbe\/evp002"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrg1471"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.01840-15"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.00042-24"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.001572"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M113.500280"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.3.803-810.2004"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2019.04.011"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.1186\/s12864-015-1584-3"},{"key":"e_1_3_4_12_2","first-page":"117","volume-title":"Advances in microbial physiology","author":"Fulton RL","year":"2023","unstructured":"Fulton RL, Downs DM. 2023. 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