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Titolo:
Identification and characterization of the sodA genes encoding manganese superoxide dismutases in Vibrio parahaemolyticus, Vibrio mimicus, and Vibriovulnificus
Autore:
Kimoto, R; Funahashi, T; Yamamoto, N; Miyoshi, S; Narimatsu, S; Yamamoto, S;
Indirizzi:
Okayama Univ, Fac Pharmaceut Sci, Okayama 7008530, Japan Okayama Univ Okayama Japan 7008530 harmaceut Sci, Okayama 7008530, Japan
Titolo Testata:
MICROBIOLOGY AND IMMUNOLOGY
fascicolo: 2, volume: 45, anno: 2001,
pagine: 135 - 142
SICI:
0385-5600(2001)45:2<135:IACOTS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; EXPRESSION; IRON; CLONING;
Keywords:
sodA; manganese superoxide dismutase; Vibrio;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, S Okayama Univ, Fac Pharmaceut Sci, 1-1-1 Tsushimanaka, Okayama 7008530, Japan Okayama Univ 1-1-1 Tsushimanaka Okayama Japan 7008530 , Japan
Citazione:
R. Kimoto et al., "Identification and characterization of the sodA genes encoding manganese superoxide dismutases in Vibrio parahaemolyticus, Vibrio mimicus, and Vibriovulnificus", MICROB IMMU, 45(2), 2001, pp. 135-142

Abstract

Sequencing of Fur titration assay-positive clones obtained from genomic DNA libraries of Vibrio parahaemolyticus, V. mimicus and V. vulnificus revealed open reading frames encoding proteins of 202, 205 and 202 amino acid residues, respectively. Each open reading frame was preceded by a predicted Fur box which overlaps a likely promoter with similarity to the -10 and -35 consensus sequence of Escherichia coli, The deduced amino acid sequences shared considerable homology with bacterial Mn-containing superoxide dismutases (MnSODs). Consistent with this, these Vibrio strains produced proteins with SOD activity resistant to inhibition by H2O2 and KCN only when grown under iron-limiting conditions. Primer extension analysis of the total RNA from these vibrios revealed iron-repressible expression of the genes. Furthermore, when grown under iron-limiting conditions, E. coli carrying a plasmid with each cloned gene overexpressed protein with the same electrophoretic mobility and insensitivity of SOD activity to H2O2 and KCN. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by N-terminal amino acidsequencing revealed that proteins (MnSODs) having N-terminal amino acid sequences consistent with those deduced from the corresponding genes were present in cell lysates of the vibrios grown under these iron-limited conditions, These results demonstrate that the genes cloned in this study are sodA homologs encoding MnSODs, whose expression is regulated by the iron status of the growth medium. PCR using a primer set based on the V. parahaemolyticus sodA sequence revealed the presence of homologous genes in certain otherVibrio species.

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Documento generato il 03/06/20 alle ore 09:41:53