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Two differentially regulated catalase genes,\n            <jats:italic>catA<\/jats:italic>\n            and\n            <jats:italic>catB<\/jats:italic>\n            , have been studied in\n            <jats:italic>Aspergillus nidulans<\/jats:italic>\n            . Here we have characterized a third catalase gene, designated\n            <jats:italic>catC<\/jats:italic>\n            , which predicts a 475-amino-acid polypeptide containing a peroxisome-targeting signal. With a molecular mass of 54 kDa, CatC shows high similarity to other small-subunit monofunctional catalases and is most closely related to catalases from other fungi,\n            <jats:italic>Archaea<\/jats:italic>\n            , and animals. In contrast, the CatA (\u223c84 kDa) and CatB (\u223c79 kDa) enzymes belong to a family of large-subunit catalases, constituting a unique fungal and bacterial group. The\n            <jats:italic>catC<\/jats:italic>\n            gene displayed a relatively constant pattern of expression, not being induced by oxidative or other types of stress. Targeted disruption of\n            <jats:italic>catC<\/jats:italic>\n            eliminated a constitutive catalase activity not detected previously in zymogram gels. However, a catalase activity detected in\n            <jats:italic>catA catB<\/jats:italic>\n            mutant strains during late stationary phase was still present in\n            <jats:italic>catC<\/jats:italic>\n            and\n            <jats:italic>catABC<\/jats:italic>\n            null mutants, thus demonstrating the presence of a fourth catalase, here named catalase D (CatD). Neither\n            <jats:italic>catC<\/jats:italic>\n            nor\n            <jats:italic>catABC<\/jats:italic>\n            triple mutants showed any developmental defect, and both mutants grew as well as wild-type strains in H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            -generating substrates, such as fatty acids, and\/or purines as the sole carbon and nitrogen sources, respectively. CatD activity was induced during late stationary phase by glucose starvation, high temperature, and, to a lesser extent, H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            treatment. The existence of at least four differentially regulated catalases indicates a large and regulated capability for H\n            <jats:sub>2<\/jats:sub>\n            O\n            <jats:sub>2<\/jats:sub>\n            detoxification in filamentous fungi.\n          <\/jats:p>","DOI":"10.1128\/jb.183.4.1434-1440.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T09:58:18Z","timestamp":1027763898000},"page":"1434-1440","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":125,"title":["Multiple Catalase Genes Are Differentially Regulated in\n            <i>Aspergillus nidulans<\/i>"],"prefix":"10.1128","volume":"183","author":[{"given":"Laura","family":"Kawasaki","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Departamento de Gene\u0301tica Molecular, Instituto de Fisiolog\u0131\u0301a Celular, Universidad Nacional Auto\u0301noma de Me\u0301xico, 04510 Me\u0301xico, D. 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