Literature DB >> 365860

An enzyme activity specific for nitrous acid-treated DNA in Escherichia coli.

K Oeda, K Shimizu, M Sekiguchi.   

Abstract

An enzyme activity specifically active on nitrous acid-treated DNA was found in an extract of Escherichia coli. The enzyme acts on both double- and single-stranded DNAs, treated with nitrous acid, in the presence of EDTA, although the former DNA is a better substrate. Evidence is presented that nitrous acid- and bisulfite-induced types of damage in DNA are recognized by different enzymes: (1) Uracil-DNA glycosylase, purified 250-fold from E. coli 1100, attacks bisulfite-treated DNA but not nitrous acid-treated DNA. (2) Almost equal levels of activity toward nitrous acid-treated DNA were found in wild-type and uracil-DNA glycosylase-deficient strains of E. coli.

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Year:  1978        PMID: 365860     DOI: 10.1093/oxfordjournals.jbchem.a132232

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Uracil-DNA glycosylase affects mismatch repair efficiency in transformation and bisulfite-induced mutagenesis in Streptococcus pneumoniae.

Authors:  V Méjean; J C Devedjian; I Rives; G Alloing; J P Claverys
Journal:  Nucleic Acids Res       Date:  1991-10-25       Impact factor: 16.971

2.  Nitrous acid damage to duplex deoxyribonucleic acid: distinction between deamination of cytosine residues and a novel mutational lesion.

Authors:  A D Frankel; B K Duncan; P E Hartman
Journal:  J Bacteriol       Date:  1980-04       Impact factor: 3.490

  2 in total

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