메뉴 건너뛰기




Volumn 186, Issue 22, 2004, Pages 7821-7825

In vivo production of active nickel superoxide dismutase from Prochlorococcus marinus MIT9313 is dependent on its cognate peptidase

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; IRON; MANGANESE; NICKEL SUPEROXIDE DISMUTASE; PEPTIDASE; SUPEROXIDE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; ZINC;

EID: 7744246514     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.22.7821-7825.2004     Document Type: Article
Times cited : (47)

References (26)
  • 2
    • 0347717645 scopus 로고    scopus 로고
    • Expression, reconstitution, and mutation of recombinant Streptomyces coelicolor NiSOD
    • Bryngelson, P. A., S. E. Arobo, J. L. Pinkham, D. E. Cabelli, and M. J. Maroney. 2004. Expression, reconstitution, and mutation of recombinant Streptomyces coelicolor NiSOD. J. Am. Chem. Soc. 126:460-461.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 460-461
    • Bryngelson, P.A.1    Arobo, S.E.2    Pinkham, J.L.3    Cabelli, D.E.4    Maroney, M.J.5
  • 3
    • 0021351387 scopus 로고
    • A hybrid superoxide dismutase containing both functional iron and manganese
    • Clare, D. A., J. Blum, and I. Fridovich. 1984. A hybrid superoxide dismutase containing both functional iron and manganese. J. Biol. Chem. 259:5932-5936.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5932-5936
    • Clare, D.A.1    Blum, J.2    Fridovich, I.3
  • 4
    • 0036279923 scopus 로고    scopus 로고
    • Substrate specificity of nickel/cobalt permeases: Insights from mutants altered in transmembrane domains I and II
    • Degen, O., and T. Eitinger. 2002. Substrate specificity of nickel/cobalt permeases: insights from mutants altered in transmembrane domains I and II. J. Bacteriol. 184:3569-3577.
    • (2002) J. Bacteriol. , vol.184 , pp. 3569-3577
    • Degen, O.1    Eitinger, T.2
  • 6
    • 0009486538 scopus 로고    scopus 로고
    • Microbial nickel transport
    • G. Winkelmann (ed.), Wiley-VCH, Weinheim, Germany
    • Eitinger, T. 2001. Microbial nickel transport, p. 397-417. In G. Winkelmann (ed.), Microbial transport systems. Wiley-VCH, Weinheim, Germany.
    • (2001) Microbial Transport Systems , pp. 397-417
    • Eitinger, T.1
  • 8
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. 1995. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 9
    • 0025353947 scopus 로고
    • Minimizing proteolysis in Escherichia coli: Genetic solutions
    • Gottesman, S. 1990. Minimizing proteolysis in Escherichia coli: genetic solutions. Methods Enzymol. 185:119-129.
    • (1990) Methods Enzymol. , vol.185 , pp. 119-129
    • Gottesman, S.1
  • 10
    • 0347753432 scopus 로고    scopus 로고
    • Heterologous production and characterization of bacterial nickel/cobalt permeases
    • Hebbeln, P., and T. Eitinger. 2004. Heterologous production and characterization of bacterial nickel/cobalt permeases. FEMS Microbiol. Lett. 230:129-135.
    • (2004) FEMS Microbiol. Lett. , vol.230 , pp. 129-135
    • Hebbeln, P.1    Eitinger, T.2
  • 12
    • 0038240674 scopus 로고    scopus 로고
    • Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
    • Kehres, D. G., and M. E. Maguire. 2003. Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. FEMS Microbiol. Rev. 27:263-290.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 263-290
    • Kehres, D.G.1    Maguire, M.E.2
  • 13
    • 0031962963 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Müller
    • Kim, E. J., H. J. Chung, B. Suh, Y. C. Hah, and J. H. Roe. 1998. Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Müller. Mol. Microbiol. 27:187-195.
    • (1998) Mol. Microbiol. , vol.27 , pp. 187-195
    • Kim, E.J.1    Chung, H.J.2    Suh, B.3    Hah, Y.C.4    Roe, J.H.5
  • 14
    • 0242552665 scopus 로고    scopus 로고
    • CbiX-homologous protein (CbiXhp), a metal-binding protein, from Streptomyces seoulensis is involved in expression of nickel-containing superoxide dismutase
    • Kim, I.-K., Y.-I. Yim, Y.-M. Kim, J.-W. Lee, H.-S. Yim, and S.-O Kang. 2003. CbiX-homologous protein (CbiXhp), a metal-binding protein, from Streptomyces seoulensis is involved in expression of nickel-containing superoxide dismutase. FEMS Microbiol. Lett. 228:21-26.
    • (2003) FEMS Microbiol. Lett. , vol.228 , pp. 21-26
    • Kim, I.-K.1    Yim, Y.-I.2    Kim, Y.-M.3    Lee, J.-W.4    Yim, H.-S.5    Kang, S.-O.6
  • 15
    • 0033286022 scopus 로고    scopus 로고
    • Diversity of superoxide-dismutases among clinical and soil isolates of Streptomyces species
    • Leclere, V., P. Boiron, and R. Blondeau. 1999. Diversity of superoxide-dismutases among clinical and soil isolates of Streptomyces species. Curr. Microbiol. 39:365-368.
    • (1999) Curr. Microbiol. , vol.39 , pp. 365-368
    • Leclere, V.1    Boiron, P.2    Blondeau, R.3
  • 16
    • 0036121256 scopus 로고    scopus 로고
    • Nickel-containing superoxide dismutase
    • Lee, J.-W., J.-H. Roe, and S.-O. Kang. 2002. Nickel-containing superoxide dismutase. Methods Enzymol. 349:90-101.
    • (2002) Methods Enzymol. , vol.349 , pp. 90-101
    • Lee, J.-W.1    Roe, J.-H.2    Kang, S.-O.3
  • 17
    • 1842583981 scopus 로고    scopus 로고
    • Superoxide dismutases: Active sites that save, but a protein that kills
    • Miller, A.-F. 2004. Superoxide dismutases: active sites that save, but a protein that kills. Curr. Opin. Chem. Biol. 8:162-168.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 162-168
    • Miller, A.-F.1
  • 19
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. 1977. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83:346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 20
    • 0029826704 scopus 로고    scopus 로고
    • Overproduction of the rbo gene product from Desulfovibrio species suppresses all deleterious effects of lack of superoxide dismutase in Eschenchia coli
    • Pianzzola, M. J., M. Soubes, and D. Touati. 1996. Overproduction of the rbo gene product from Desulfovibrio species suppresses all deleterious effects of lack of superoxide dismutase in Eschenchia coli. J. Bacteriol. 178:6736-6742.
    • (1996) J. Bacteriol. , vol.178 , pp. 6736-6742
    • Pianzzola, M.J.1    Soubes, M.2    Touati, D.3
  • 22
    • 0025025875 scopus 로고
    • Identification of catalytic residues in the beta-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross-reactivity between the beta-glucoside and glucose systems
    • Schnetz, K., S. L. Sutrina, M. H. Saier, and B. Rak. 1990. Identification of catalytic residues in the beta-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross-reactivity between the beta-glucoside and glucose systems. J. Biol. Chem. 265:13464-13471.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13464-13471
    • Schnetz, K.1    Sutrina, S.L.2    Saier, M.H.3    Rak, B.4
  • 26


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.