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To further understand the physiological consequences of flux alterations at this point in metabolism,\n            <jats:italic>Escherichia coli<\/jats:italic>\n            genes whose expression was induced by partial inhibition of ALS were sought. Plasmid-based fusions of random\n            <jats:italic>E. coli<\/jats:italic>\n            DNA fragments to\n            <jats:italic>Photorhabdus luminescens luxCDABE<\/jats:italic>\n            were screened for bioluminescent increases in actively growing liquid cultures slowed 25% by the addition of SM. From more than 8,000 transformants, 12 unique SM-inducible promoter-\n            <jats:italic>lux<\/jats:italic>\n            fusions were identified. The\n            <jats:italic>lux<\/jats:italic>\n            reporter genes were joined to seven uncharacterized open reading frames,\n            <jats:italic>f253a<\/jats:italic>\n            ,\n            <jats:italic>f415<\/jats:italic>\n            ,\n            <jats:italic>frvX<\/jats:italic>\n            ,\n            <jats:italic>o513<\/jats:italic>\n            ,\n            <jats:italic>o521<\/jats:italic>\n            ,\n            <jats:italic>yciG<\/jats:italic>\n            , and\n            <jats:italic>yohF<\/jats:italic>\n            , and five known genes,\n            <jats:italic>inaA<\/jats:italic>\n            ,\n            <jats:italic>ldcC<\/jats:italic>\n            ,\n            <jats:italic>osmY<\/jats:italic>\n            ,\n            <jats:italic>poxB<\/jats:italic>\n            , and\n            <jats:italic>sohA<\/jats:italic>\n            . Inactivation of the\n            <jats:italic>rpoS<\/jats:italic>\n            -encoded sigma factor, \u03c2\n            <jats:sup>S<\/jats:sup>\n            , reduced basal expression levels of six of these fusions 10- to 200-fold. These six genes defined four new members of the \u03c2\n            <jats:sup>S<\/jats:sup>\n            regulon,\n            <jats:italic>f253a<\/jats:italic>\n            ,\n            <jats:italic>ldcC<\/jats:italic>\n            ,\n            <jats:italic>yciG<\/jats:italic>\n            , and\n            <jats:italic>yohF<\/jats:italic>\n            , and included two known members,\n            <jats:italic>osmY<\/jats:italic>\n            and\n            <jats:italic>poxB<\/jats:italic>\n            . Furthermore, the weak acid salicylate, which causes cytoplasmic acidification, also induced increased bioluminescence from seven SM-inducible promoter-\n            <jats:italic>lux<\/jats:italic>\n            fusion-containing strains, namely, those with fusions of the \u03c2\n            <jats:sup>S<\/jats:sup>\n            -controlled genes and\n            <jats:italic>inaA<\/jats:italic>\n            . The pattern of gene expression changes suggested that restricted ALS activity may result in intracellular acidification and induction of the \u03c2\n            <jats:sup>S<\/jats:sup>\n            -dependent stress response.\n          <\/jats:p>","DOI":"10.1128\/jb.180.4.785-792.1998","type":"journal-article","created":{"date-parts":[[2019,12,31]],"date-time":"2019-12-31T16:31:49Z","timestamp":1577809909000},"page":"785-792","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":50,"title":["Constricted Flux through the Branched-Chain Amino Acid Biosynthetic Enzyme Acetolactate Synthase Triggers Elevated Expression of Genes Regulated by\n            <i>rpoS<\/i>\n            and Internal Acidification"],"prefix":"10.1128","volume":"180","author":[{"given":"Tina K.","family":"Van Dyk","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Central Research and Development Department, DuPont Co., Wilmington, Delaware 19880-0173,1 and"},{"name":"<!--label omitted: 2-->Department of Animal and Food Sciences, University of Delaware, Newark, Delaware 19717-13032"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brenda L.","family":"Ayers","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Central Research and Development Department, DuPont Co., Wilmington, Delaware 19880-0173,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robin W.","family":"Morgan","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Department of Animal and Food Sciences, University of Delaware, Newark, Delaware 19717-13032"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert A.","family":"Larossa","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Central Research and Development Department, DuPont Co., Wilmington, Delaware 19880-0173,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1021\/bp00034a019","article-title":"Metabolic engineering of Escherichia coli to enhance recombinant protein production through acetate reduction","volume":"11","author":"Aristidou A. 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