Abstract
In this study, the whole genome of Streptomyces peucetius ATCC 27952 was analyzed and two superoxide dismutases (SODs), named sp-sod1 and sp-sod2, were identified. The sp-sod1 is a putative Fe-Zn sod that is 636 bp in length. The sp-sod2 is a putative NiSOD that is 396 bp in length. The deduced amino acid sequence of sp-sod1 shared approximately 85 ∼ 90% identity with the iron sod of S. griseus, S. coelicolor A3(2), and S. avermitilis MA-4680 whereas sp-sod2 shared approximately 87 ∼ 94% identity with S. avermitilis, S. coelicolor A3(2) and S. seoulensis. The sp-sod1 was characterized to be FeSOD in the sod mutant E. coli QC871. The N-terminal deleted sp-sod2 along with a putative signal peptidase sp-sodX, which was immediately downstream, was co-expressed in E. coli. This recombinant E. coli strain did not produce the processed mature Sp-SOD2 unlike S. coelicolor Muller. However, Sp-SOD2 was confirmed to be NiSOD in S. lividans TK24.
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