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H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    can penetrate membranes and damage key intracellular biomolecules, including DNA and iron-dependent enzymes. Bacteria defend themselves against this H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    by inducing a regulon that engages multiple defensive strategies. A previous microarray study suggested that\n                    <jats:italic>yaaA<\/jats:italic>\n                    , an uncharacterized gene found in many bacteria, was induced by H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    in\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                    as part of its OxyR regulon. Here we confirm that\n                    <jats:italic>yaaA<\/jats:italic>\n                    is a key element of the stress response to H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    . In a catalase\/peroxidase-deficient (Hpx\n                    <jats:sup>\u2212<\/jats:sup>\n                    ) background,\n                    <jats:italic>yaaA<\/jats:italic>\n                    deletion mutants grew poorly, filamented extensively, and lost substantial viability when they were cultured in aerobic LB medium. The results from a\n                    <jats:italic>thyA<\/jats:italic>\n                    forward mutagenesis assay and the growth defect of the\n                    <jats:italic>yaaA<\/jats:italic>\n                    deletion in a recombination-deficient (\n                    <jats:italic>recA56<\/jats:italic>\n                    ) background indicated that\n                    <jats:italic>yaaA<\/jats:italic>\n                    mutants accumulated high levels of DNA damage. The growth defect of\n                    <jats:italic>yaaA<\/jats:italic>\n                    mutants could be suppressed by either the addition of iron chelators or mutations that slowed iron import, indicating that the DNA damage was caused by the Fenton reaction. Spin-trapping experiments confirmed that Hpx\n                    <jats:sup>\u2212<\/jats:sup>\n                    <jats:italic>yaaA<\/jats:italic>\n                    cells had a higher hydroxyl radical (HO\n                    <jats:sup>\u2022<\/jats:sup>\n                    ) level. Electron paramagnetic resonance spectroscopy analysis showed that the proximate cause was an unusually high level of intracellular unincorporated iron. These results demonstrate that during periods of H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    stress the induction of YaaA is a critical device to suppress intracellular iron levels; it thereby attenuates the Fenton reaction and the DNA damage that would otherwise result. The molecular mechanism of YaaA action remains unknown.\n                  <\/jats:p>","DOI":"10.1128\/jb.00001-11","type":"journal-article","created":{"date-parts":[[2011,3,5]],"date-time":"2011-03-05T08:51:34Z","timestamp":1299315094000},"page":"2186-2196","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":81,"title":["The YaaA Protein of the Escherichia coli OxyR Regulon Lessens Hydrogen Peroxide Toxicity by Diminishing the Amount of Intracellular Unincorporated Iron"],"prefix":"10.1128","volume":"193","author":[{"given":"Yuanyuan","family":"Liu","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana, Illinois 61801"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah C.","family":"Bauer","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana, Illinois 61801"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Imlay","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Illinois, Urbana, Illinois 61801"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.130.1.187-191.1977"},{"key":"e_1_3_3_3_2","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1111\/j.1365-2958.2009.06699.x","article-title":"Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli","volume":"72","author":"Anjem A.","year":"2009","unstructured":"AnjemA. 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