Recombination is essential for viability of an Escherichia coli dam (DNA adenine methyltransferase) mutant
Department of Pharmacology
Bacterial Proteins; Base Pair Mismatch; Crosses, Genetic; *DNA Helicases; DNA Repair; DNA-Binding Proteins; Endodeoxyribonucleases; Escherichia coli; *Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; *Mutation; Rec A Recombinases; *Recombination, Genetic; SOS Response (Genetics); Site-Specific DNA-Methyltransferase (Adenine-Specific)
Life Sciences | Medicine and Health Sciences
Double mutants of Escherichia coli dam (DNA adenine methyltransferase) strains with ruvA, ruvB, or ruvC could not be constructed, whereas dam derivatives with recD, recF, recJ, and recR were viable. The ruv gene products are required for Holliday junction translocation and resolution of recombination intermediates. A dam recG (Holliday junction translocation) mutant strain was isolated but at a very much lower frequency than expected. The inviability of a dam lexA (Ind(-)) host was abrogated by the simultaneous presence of plasmids encoding both recA and ruvAB. This result indicates that of more than 20 SOS genes, only recA and ruvAB need to be derepressed to allow for dam mutant survival. The presence of mutS or mutL mutations allowed the construction of dam lexA (Ind(-)) derivatives. The requirement for recA, recB, recC, ruvA, ruvB, ruvC, and possibly recG gene expression indicates that recombination is essential for viability of dam bacteria probably to repair DNA double-strand breaks. The effect of mutS and mutL mutations indicates that DNA mismatch repair is the ultimate source of most of these DNA breaks. The requirement for recombination also suggests an explanation for the sensitivity of dam cells to certain DNA-damaging agents.
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Citation: J Bacteriol. 2000 Jan;182(2):463-8.
Journal of bacteriology
Marinus, Martin G., "Recombination is essential for viability of an Escherichia coli dam (DNA adenine methyltransferase) mutant" (2000). Open Access Articles. 658.