{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,24]],"date-time":"2026-07-24T18:59:55Z","timestamp":1784919595839,"version":"3.55.0"},"reference-count":0,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2003,10,31]],"date-time":"2003-10-31T00:00:00Z","timestamp":1067558400000},"content-version":"vor","delay-in-days":2221,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[1997,10]]},"abstract":"<jats:p>We have identified and functionally characterized a new <jats:italic>Escherichia coli<\/jats:italic> gene, <jats:italic>dsbG<\/jats:italic>, whose product is involved in disulphide bond formation in the periplasm. The <jats:italic>dsbG<\/jats:italic> gene was cloned from a multicopy plasmid library lacking the <jats:italic>dsbB<\/jats:italic> redox protein\u2010encoding gene. Multicopy <jats:italic>dsbG<\/jats:italic>\u2010carrying clones were selected, since they allowed <jats:italic>E. coli<\/jats:italic> to grow at lethal concentrations of dithiothreitol. In a complementary genetic approach, point mutations were independently obtained and mapped to the <jats:italic>dsbG<\/jats:italic> gene. Such mutations led simultaneously to a dithiothreitol\u2010sensitive phenotype and an increased \u03c3<jats:sup>E<\/jats:sup>\u2010dependent heat shock response, which reflects the presence of misfolded proteins in the extracytoplasm. In agreement with these observations, <jats:italic>dsbG<\/jats:italic> mutants were shown to accumulate reduced forms of a variety of disulphide bond\u2010containing proteins in the periplasm. This DsbG defect could be rescued by addition to the growth medium of either oxidized dithiothreitol or cystine, or by overexpression of the <jats:italic>dsbA<\/jats:italic> or <jats:italic>dsbB<\/jats:italic> genes. DsbG is synthesized as a precursor form of 27.5\u2003kDa and processed to a 25.7\u2003kDa mature species located in the periplasm. DsbG was overproduced, purified to homogeneity and shown to have redox properties of thiol\u2013disulphide oxidoreductases <jats:italic>in vitro<\/jats:italic>. Replacement of the first Cys residue of the predicted active site, Phe\u2013(Xaa)<jats:sub>4<\/jats:sub>\u2013Cys\u2013Pro\u2013Tyr\u2013Cys by Ala, completely inactivated DsbG protein function. Taken together, all our results demonstrate that DsbG acts <jats:italic>in vivo<\/jats:italic> as an efficient thiol\u2013disulphide oxidase. In addition, <jats:italic>dsbG<\/jats:italic> is the first member of the <jats:italic>dsb<\/jats:italic> family for which null mutations are conditionally lethal and can be propagated only if supplemented with oxidants in the growth medium. We propose that the main role of DsbG is to maintain the proper redox balance between the DsbA\/DsbB and DsbC systems.<\/jats:p>","DOI":"10.1046\/j.1365-2958.1997.5581925.x","type":"journal-article","created":{"date-parts":[[2003,11,2]],"date-time":"2003-11-02T17:45:19Z","timestamp":1067795119000},"page":"121-132","source":"Crossref","is-referenced-by-count":98,"title":["A new <i>Escherichia coli<\/i> gene, <i>dsbG<\/i>, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA\/DsbB and DsbC redox proteins"],"prefix":"10.1111","volume":"26","author":[{"given":"Catherine L.","family":"Andersen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"Matthey\u2010Dupraz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Missiakas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Satish","family":"Raina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2003,10,31]]},"container-title":["Molecular Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1046%2Fj.1365-2958.1997.5581925.x","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1046\/j.1365-2958.1997.5581925.x","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1046\/j.1365-2958.1997.5581925.x","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,11]],"date-time":"2023-09-11T12:11:29Z","timestamp":1694434289000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1046\/j.1365-2958.1997.5581925.x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,10]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1997,10]]}},"alternative-id":["10.1046\/j.1365-2958.1997.5581925.x"],"URL":"https:\/\/doi.org\/10.1046\/j.1365-2958.1997.5581925.x","archive":["Portico"],"relation":{},"ISSN":["0950-382X","1365-2958"],"issn-type":[{"value":"0950-382X","type":"print"},{"value":"1365-2958","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,10]]}}}