CLONING OF A SUPEROXIDE-DISMUTASE GENE FROM LISTERIA-IVANOVII BY FUNCTIONAL COMPLEMENTATION IN ESCHERICHIA-COLI AND CHARACTERIZATION OF THE GENE-PRODUCT

被引：11

作者：

HAAS, A ^{[1
]}

GOEBEL, W ^{[1
]}

机构：

[1] UNIV WURZBURG, INST GENET & MIKROBIOL, RONTGENRING 11, W-8700 WURZBURG, GERMANY

来源：

MOLECULAR AND GENERAL GENETICS | 1992年 / 231卷 / 02期

关键词：

LISTERIA-IVANOVII; SUPEROXIDE DISMUTASE; COMPLEMENTATION; HYBRID ENZYMES; PATHOGENICITY;

D O I：

10.1007/BF00279805

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A gene encoding superoxide dismutase (EC 1.15.1.1., SOD) was isolated from a plasmid library of chromosomal DNA from Listeria ivanovii by functional complementation of an SOD-negative Escherichia coli host. The nucleotide sequence of the cloned gene was determined and contained an open reading frame which codes for a protein of 202 amino acid residues (calculated molecular weight 22755 Da including the amino-terminal methionine residue). Comparison of the deduced amino acid sequence of L. ivanovii SOD with previously reported SOD amino acid sequences revealed considerable homologies with Fe- and Mn-dependent SODs. Enzymatic analyses using cell lysates and the purified recombinant enzyme indicated that this SOD is manganese-dependent. The recombinant SOD accounted for up to 30% of the total soluble protein in recombinant E. coli and protected sodA sodB mutants against the toxic effects of paraquat. Subunits of the recombinant Listeria SOD and of both E. coli SODs formed enzymatically active hybrids in vivo.

引用

页码：313 / 322

页数：10

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