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Serratia marcescens rpr gene sensitizes Escherichia coli wild‐type, xth , and nfo strains to methyl methanesulphonate
Author(s) -
Murphy K. E.,
Braymer H. D.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00634.x
Subject(s) - escherichia coli , biology , serratia marcescens , complementation , enterobacteriaceae , microbiology and biotechnology , wild type , dna (apurinic or apyrimidinic site) lyase , gene , endonuclease , genetics , mutant , ap site
Summary It is reported here that the rpr DNA repair gene of Serratia marcescens does not complement an Escherichia coli xth nfo AP endonuclease mutation for resistance to methyl methanesulphonate (MMS). Rather, rpr sensitized Escherichia coli wild‐type, xth , and nfo strains to MMS. Also, it was found that rpr could not complement a triple tag alkA recA mutation in E. coli , indicating that there are limits to rpr complementing capabilities. It was determined that rpr gene dosage was not a factor in recA complementation. MMS sensitization of an E. coli wild‐type strain, however, was directly related to rpr copy number. These data indicate that Rpr does not have an associated AP endonuclease activity, and that it is incapable of substituting for Tag I, Tag II, and RecA in a tag alkA recA background.