Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for the meningococcal viability

Abstract : TlpAs are bacterial thioredoxin-like periplasmic disulfide oxidoreductases generally involved in cytochrome c maturation 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 thioredoxin-like protein, called TlpA2. Biochemical and kinetic characterizations of the soluble form of TlpA2, tTlpA2, were performed. A reduction potential of -0.230 V at pH 7 was calculated, suggesting that TlpA2 acts as a reductant in the oxidative environment of the periplasm. Using a second-order reactive probe, high p K app 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\textquoteright 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 B. pertussis CcsX mutant. Together, these data support an essential role of TlpA2 in the cytochrome c maturation process in N. meningitidis .
Type de document :
Article dans une revue
Biochemical Journal, Portland Press, 2015, 〈10.1042/BJ20140868〉
Liste complète des métadonnées

https://hal.univ-lorraine.fr/hal-01451679
Contributeur : Imopa Ul <>
Soumis le : mercredi 1 février 2017 - 12:33:41
Dernière modification le : jeudi 22 février 2018 - 14:34:02

Identifiants

Collections

Citation

Adeline Gand, Laure Selme-Roussel, Sabrina Collin, Guy Branlant, Christophe Jacob, et al.. Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for the meningococcal viability. Biochemical Journal, Portland Press, 2015, 〈10.1042/BJ20140868〉. 〈hal-01451679〉

Partager

Métriques

Consultations de la notice

34