{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T20:07:40Z","timestamp":1774296460793,"version":"3.50.1"},"reference-count":46,"publisher":"Microbiology Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,3,1]]},"abstract":"<jats:p><jats:italic>Porphyromonas gingivalis<\/jats:italic>, an obligately anaerobic bacterium, is implicated as a major pathogen in the development and progression of chronic periodontitis. Although expression of several virulence factors of the bacterium has been found to be affected by environmental stress such as entrance into the stationary growth phase and heat, there is relatively little information on the mechanisms that may operate in the bacterium in response to environmental stress. In this study, a novel protein (UstA) was investigated that was initially identified following two-dimensional gel analysis. Expression of UstA was upregulated in stationary phase or by exposure to atmospheric oxygen. N-terminal sequencing and database analysis with the<jats:italic>P. gingivalis<\/jats:italic>genome sequence revealed that the UstA-encoding gene (<jats:italic>ustA<\/jats:italic>) was located upstream of a homologue of the<jats:italic>usp<\/jats:italic>gene encoding the universal stress protein on the chromosome. The<jats:italic>ustA<\/jats:italic>gene appeared to be transcribed in a monocistronic fashion, as revealed by primer extension and Northern blot analysis. To elucidate the role of UstA in the bacterium, chromosomal mutants carrying a disruption of the<jats:italic>ustA<\/jats:italic>gene were constructed. The<jats:italic>ustA<\/jats:italic>mutant grew slower than the wild-type parent strain in rich medium, resulting in a lower yield in stationary phase. Furthermore, in this mutant, expression levels of the<jats:italic>P. gingivalis<\/jats:italic>homologues of superoxide dismutase, thiol peroxidase and thioredoxin were markedly higher than those in the wild-type, especially in stationary phase. The<jats:italic>ustA<\/jats:italic>mutant was more resistant to diamide, a thiol-specific oxidant, than the wild-type. In addition, the<jats:italic>ustA<\/jats:italic>mutation suppressed hypersensitivities of the<jats:italic>oxyR<\/jats:italic>mutant to diamide, metronidazole and mitomycin C. These results suggest that UstA may play a significant role in oxidative stress responses in the bacterium.<\/jats:p>","DOI":"10.1099\/mic.0.27589-0","type":"journal-article","created":{"date-parts":[[2005,3,10]],"date-time":"2005-03-10T10:44:29Z","timestamp":1110451469000},"page":"841-853","source":"Crossref","is-referenced-by-count":26,"title":["Novel stationary-phase-upregulated protein of Porphyromonas gingivalis influences production of superoxide dismutase, thiol peroxidase and thioredoxin"],"prefix":"10.1099","volume":"151","author":[{"given":"Yuichiro","family":"Kikuchi","sequence":"first","affiliation":[{"name":"Division of Microbiology and Oral Infection, Department of Developmental and Reconstructive Medicine, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoya","family":"Ohara","sequence":"additional","affiliation":[{"name":"Division of Microbiology and 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