Identification of Two Superoxide Dismutases (FeSOD and NiSOD) from Streptomyces peucetius ATCC 27952

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 amin...

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Veröffentlicht in:Biotechnology and bioprocess engineering 2010, 15(5), , pp.785-792
Hauptverfasser: Kanth, Bashistha Kumar, SunMoon University, Asan, Republic of Korea, Oh, T.J., SunMoon University, Asan, Republic of Korea, Sohng, J.K., SunMoon University, Asan, Republic of Korea
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Sprache:eng
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Zusammenfassung: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.
ISSN:1226-8372
1976-3816
DOI:10.1007/s12257-010-0009-z