Document Detail


Identification of a segment of DsbB essential for its respiration-coupled oxidation.
MedLine Citation:
PMID:  11123697     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 now show 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.
Authors:
T Kobayashi; Y Takahashi; K Ito
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular microbiology     Volume:  39     ISSN:  0950-382X     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2001 Jan 
Date Detail:
Created Date:  2001-02-20     Completed Date:  2001-02-22     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  158-65     Citation Subset:  IM    
Affiliation:
Institute for Virus Research and CREST, Japan Science and Technology Corporation, Kyoto University, Kyoto 606-8507, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / genetics,  metabolism*
Dithiothreitol / pharmacology
Drug Resistance, Microbial
Membrane Proteins / genetics,  metabolism*
Molecular Sequence Data
Mutagenesis, Insertional
Mutation
Oxidation-Reduction
Oxidoreductases / metabolism*
Oxygen Consumption
Protein Conformation
Protein Disulfide-Isomerases / metabolism
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/DsbB protein, Bacteria; 0/Membrane Proteins; 3483-12-3/Dithiothreitol; EC 1.-/Oxidoreductases; EC 5.3.4.1/Protein Disulfide-Isomerases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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