{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,6,12]],"date-time":"2024-06-12T23:37:18Z","timestamp":1718235438149},"reference-count":47,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2015,6,1]]},"abstract":"<jats:p>TlpAs (thioredoxin-like proteins) are bacterial thioredoxin-like periplasmic disulfide oxidoreductases generally involved in cytochrome c maturation (Ccm) process. They contain a characteristic CXXC active site motif involved in disulfide exchange reaction. In the human pathogenic Neisseria meningitidis species, no TlpA has been characterized so far. In the present study, using an in silico analysis, we identified a putative periplasmic TlpA, called TlpA2. Biochemical and kinetic characterizations of the soluble form of TlpA2, tTlpA2 (truncated TlpA2), were performed. A reduction potential of \u22120.230\u00a0V at pH\u00a07 was calculated, suggesting that TlpA2 acts as a reductant in the oxidative environment of the periplasm. Using a second-order reactive probe, high pKapp (apparent pKa) values were determined for the two cysteines of the SCXXC motif. The tTlpA2 was shown to be efficiently reduced by the N-terminal domain of the DsbD, whereas tTlpA2 reduced a mimetic peptide of cytochrome c\u2032 with a catalytic efficiency similar to that observed with other disulfide oxidoreductase like ResA. Moreover, the corresponding gene tlpA2 was shown to be essential for the pathogen viability and able to partially complement a Bordetella pertussis CcsX mutant. Together, these data support an essential role of TlpA2\u00a0in the Ccm process in N.\u00a0meningitidis.<\/jats:p>","DOI":"10.1042\/bj20140868","type":"journal-article","created":{"date-parts":[[2015,4,1]],"date-time":"2015-04-01T17:00:37Z","timestamp":1427907637000},"page":"271-282","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from <i>Neisseria meningitidis<\/i> essential for meningococcal viability"],"prefix":"10.1042","volume":"468","author":[{"given":"Adeline","family":"Gand","sequence":"first","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laure","family":"Selme-Roussel","sequence":"additional","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sabrina","family":"Collin","sequence":"additional","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guy","family":"Branlant","sequence":"additional","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christophe","family":"Jacob","sequence":"additional","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sandrine","family":"Boschi-Muller","sequence":"additional","affiliation":[{"name":"IMoPA, \u00c9quipe Enzymologie Mol\u00e9culaire et Structurale, UMR 7365 CNRS-Universit\u00e9 de Lorraine, B\u00e2timent Biop\u00f4le, Facult\u00e9 de M\u00e9decine, 9 avenue de la Fore\u00e2t de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2015,5,22]]},"reference":[{"key":"2021112216181529200_B1","doi-asserted-by":"publisher","first-page":"13981","DOI":"10.1021\/bi048947r","article-title":"Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor","volume":"43","author":"Copley","year":"2004","journal-title":"Biochemistry"},{"key":"2021112216181529200_B2","doi-asserted-by":"publisher","first-page":"3516","DOI":"10.1074\/jbc.M311833200","article-title":"Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. 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