{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T13:43:30Z","timestamp":1790257410851,"version":"4.1.0"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"16","license":[{"start":{"date-parts":[[2000,8,15]],"date-time":"2000-08-15T00:00:00Z","timestamp":966297600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2000,8,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A\n            <jats:italic>Pseudomonas aeruginosa oxyR<\/jats:italic>\n            mutant was dramatically sensitive to H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            , despite possessing wild-type catalase activity. Oxygen-dependent\n            <jats:italic>oxyR<\/jats:italic>\n            phenotypes also included an inability to survive aerobic serial dilution in Luria broth and to resist aminoglycosides. Plating the\n            <jats:italic>oxyR<\/jats:italic>\n            mutant after serial dilution in its own spent culture supernatant, which contained the major catalase KatA, or under anaerobic conditions allowed for survival. KatA was resistant to sodium dodecyl sulfate, proteinase K, pepsin, trypsin, chymotrypsin and the neutrophil protease cathepsin G. When provided in\n            <jats:italic>trans<\/jats:italic>\n            and expressed constitutively, the OxyR-regulated genes\n            <jats:italic>katB<\/jats:italic>\n            ,\n            <jats:italic>ahpB<\/jats:italic>\n            , and\n            <jats:italic>ahpCF<\/jats:italic>\n            could not restore both the serial dilution defect and H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            resistance; only\n            <jats:italic>oxyR<\/jats:italic>\n            itself could do so. The aerobic dilution defect could be complemented, in part, by only\n            <jats:italic>ahpB<\/jats:italic>\n            and\n            <jats:italic>ahpCF<\/jats:italic>\n            , suggesting that the latter gene products could possess a catalase-like activity. Aerobic Luria broth was found to generate \u223c1.2 \u03bcM H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            min\n            <jats:sup>\u22121<\/jats:sup>\n            via autoxidation, a level sufficient to kill serially diluted\n            <jats:italic>oxyR<\/jats:italic>\n            and\n            <jats:italic>oxyR katA<\/jats:italic>\n            bacteria and explain the molecular mechanism behind the aerobic serial dilution defect. Taken together, our results indicate that inactivation of OxyR renders\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            exquisitely sensitive to both H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            and aminoglycosides, which are clinically and environmentally important antimicrobials.\n          <\/jats:p>","DOI":"10.1128\/jb.182.16.4557-4563.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:00:58Z","timestamp":1027764058000},"page":"4557-4563","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":90,"title":["A Protease-Resistant Catalase, KatA, Released upon Cell Lysis during Stationary Phase Is Essential for Aerobic Survival of a\n            <i>Pseudomonas aeruginosa oxyR<\/i>\n            Mutant at Low Cell Densities"],"prefix":"10.1128","volume":"182","author":[{"given":"Daniel J.","family":"Hassett","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Molecular Genetics, Biochemistry and Microbiology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eyad","family":"Alsabbagh","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Molecular Genetics, Biochemistry and Microbiology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kislay","family":"Parvatiyar","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Molecular Genetics, Biochemistry and Microbiology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael L.","family":"Howell","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Protein Express, Inc., Cincinnati, Ohio 452192; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert W.","family":"Wilmott","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Division of Pulmonary Medicine, Allergy and Clinical Immunology, Department of Pediatrics,3University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Urs A.","family":"Ochsner","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Department of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 802624"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1111\/j.1365-2958.1994.tb00421.x","article-title":"The dps promoter is activated by OxyR during growth and by IHF and \u03c2S in stationary phase","volume":"13","author":"Altuvia S.","year":"1994","unstructured":"Altuvia S. 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