Affiliation:
1. Department of Biotechnology, Faculty of Engineering,1 and
2. High-Technology Research Center,2 Kansai University, Suita, Osaka 564, Japan
Abstract
ABSTRACT
Bacillus subtilis
was found to possess one detectable superoxide dismutase (Sod) in both vegetative cells and spores. The Sod activity in vegetative cells was maximal at stationary phase. Manganese was necessary to sustain Sod activity at stationary phase, but paraquat, a superoxide generator, did not induce the expression of Sod. The specific activity of purified Sod was approximately 2,600 U/mg of protein, and the enzyme was a homodimer protein with a molecular mass of approximately 25,000 per monomer. The gene encoding Sod, designated
sodA
, was cloned by the combination of several PCR methods and the Southern hybridization method. DNA sequence analysis revealed the presence of one open reading frame consisting of 606 bp. Several putative promoter sites were located in the upstream region of
sodA
. The deduced amino acid sequence showed high homology with other bacterial manganese Sods. Conserved regions in bacterial manganese Sod could also be seen. The phenotype of double mutant
Escherichia coli sodA sodB
, which could not grow in minimal medium without supplemental amino acids, was complemented by the expression of
B. subtilis sodA
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
49 articles.
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