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Titolo:
Identification of a segment of DsbB essential for its respiration-coupled oxidation
Autore:
Kobayashi, T; Takahashi, Y; Ito, K;
Indirizzi:
Kyoto Univ, Inst Virus Res, Kyoto 6068507, Japan Kyoto Univ Kyoto Japan 6068507 niv, Inst Virus Res, Kyoto 6068507, Japan Kyoto Univ, Japan Sci & Technol Corp, CREST, Kyoto 6068507, Japan Kyoto Univ Kyoto Japan 6068507 Technol Corp, CREST, Kyoto 6068507, Japan
Titolo Testata:
MOLECULAR MICROBIOLOGY
fascicolo: 1, volume: 39, anno: 2001,
pagine: 158 - 165
SICI:
0950-382X(200101)39:1<158:IOASOD>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
DISULFIDE BOND FORMATION; ESCHERICHIA-COLI; ACTIVE-SITE; CYSTEINE RESIDUES; CXXC MOTIF; PERIPLASM; PROTEINS; CATALYST; PATHWAY; STATES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Ito, K Kyoto Univ, Inst Virus Res, Kyoto 6068507, Japan Kyoto Univ KyotoJapan 6068507 st Virus Res, Kyoto 6068507, Japan
Citazione:
T. Kobayashi et al., "Identification of a segment of DsbB essential for its respiration-coupled oxidation", MOL MICROB, 39(1), 2001, pp. 158-165

Abstract

In the Escherichia coli protein disulphide bond formation pathway, membrane-bound DsbB oxidizes periplasmic DsbA, the disulphide bond-introducing enzyme. The Cys-41-Val-Leu-Cys-44 motif in the first periplasmic domain of DsbB is kept strongly oxidized by the respiratory function of the cell. We nowshow that the characteristic dithiothreitol resistance of the Cys-41-Cys-44 bond was retained even when the flanked Val-Leu combination was replaced by XX sequences from other oxidoreductases. Results of insertion mutagenesis showed that only the insertions (1-31 amino acids) in the region C-terminally adjacent to the CXXC motif impaired the oxidized state of DsbB. Deletion of a single amino acid from this region also rendered DsbB reduced and inactive. However, single amino acid substitutions of the four residues flanked by CXXC and the transmembrane segment did not abolish the oxidation of DsbB. These results suggest that some physical property, such as distance of the CXXC motif from the membrane, is important for the respiration-coupled oxidation of DsbB.

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Documento generato il 30/03/20 alle ore 00:50:03