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PMID: 7836310 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cloning and characterization of the gene for a protein thiol-disulfide oxidoreductase in Bacillus brevis.

Journal of bacteriology ·Vol. 177 ·No. 3 ·1995-02-00 ·Pages 745-9

Ishihara T, Tomita H, Hasegawa Y, Tsukagoshi N, Yamagata H, Udaka S

Abstract

The gene (bdb) for protein thiol-disulfide oxidoreductase cloned from Bacillus brevis was found to encode a polypeptide consisting of 117 amino acid residues with a signal peptide of 27 residues. Bdb contains a well-conserved motif, Cys-X-X-Cys, which functions as the active center of disulfide oxidoreductases such as DsbA, protein disulfide isomerase, and thioredoxin. The deduced amino acid sequence showed significant homology with those of several bacterial thioredoxins. The bdb gene complemented the Escherichia coli dsbA mutation, restoring motility by means of flagellar and alkaline phosphatase activity. The Bdb protein overproduced in B. brevis was enzymatically active in both reduction and oxidization of disulfide bonds in vitro. Immunoblotting indicated that Bdb could function at the periphery of the cell.

Related Genes
bdb
MeSH Terms
Amino Acid Sequence Bacillus/enzymology,genetics Base Sequence Blotting, Western Cloning, Molecular Gene Expression Regulation, Bacterial Genes, Bacterial Glutaredoxins Molecular Sequence Data Oxidoreductases/genetics,isolation & purification,physiology Protein Disulfide Reductase (Glutathione)
Chemicals
Glutaredoxins Oxidoreductases Protein Disulfide Reductase (Glutathione)
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Ishihara T
Department of Applied Biological Sciences, Faculty of Agriculture, Nagoya University, Japan.
Tomita H
Hasegawa Y
Tsukagoshi N
Yamagata H
Udaka S
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.177.3.745-749.1995
Published
1995-02-00
Pages
745-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC176652
Subset
IM
Databases
GENBANK
D37936
External Links
PubMed source DOI: 10.1128/jb.177.3.745-749.1995 PMC Full Text View journal details
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