title: Suppression of the E. coli SOS response by dNTP pool changes.
abstract: The Escherichia coli SOS system is a well-established model for the cellular response to DNA damage. Control of SOS depends largely on the RecA protein. When RecA is activated by single-stranded DNA in the presence of a nucleotide triphosphate cofactor, it mediates cleavage of the LexA repressor, leading to expression of the 30(+)-member SOS regulon. RecA activation generally requires the introduction of DNA damage. However, certain recA mutants, like recA730, bypass this requirement and display constitutive SOS expression as well as a spontaneous (SOS) mutator effect. Presently, we investigated the possible interaction between SOS and the cellular deoxynucleoside triphosphate (dNTP) pools. We found that dNTP pool changes caused by deficiencies in the ndk or dcd genes, encoding nucleoside diphosphate kinase and dCTP deaminase, respectively, had a strongly suppressive effect on constitutive SOS expression in recA730 strains. The suppression of the recA730 mutator effect was alleviated in a lexA-deficient background. Overall, the findings suggest a model in which the dNTP alterations in the ndk and dcd strains interfere with the activation of RecA, thereby preventing LexA cleavage and SOS induction.
authors.affiliation: Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106, Warsaw, Poland.
authors.forename: Katarzyna H
authors.initials: KH
authors.lastname: Maslowska
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106, Warsaw, Poland.
authors.forename: Karolina
authors.initials: K
authors.lastname: Makiela-Dzbenska
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106, Warsaw, Poland.
authors.forename: Iwona J
authors.initials: IJ
authors.lastname: Fijalkowska
authors.affiliation: Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA schaaper@niehs.nih.gov.
authors.forename: Roel M
authors.initials: RM
authors.lastname: Schaaper
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D003854:Deoxyribonucleotides / Q000378:metabolism*; D024881:Drug Resistance, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D016296:Mutagenesis; D009154:Mutation; D009701:Nucleoside-Diphosphate Kinase / Q000235:genetics; D009709:Nucleotide Deaminases / Q000235:genetics; D011938:Rec A Recombinases / Q000235:genetics; D018085:Regulon; D012293:Rifampin / Q000494:pharmacology; D013014:SOS Response, Genetics; D012697:Serine Endopeptidases / Q000235:genetics; D013489:Suppression, Genetic; D000099160:LexA Repressor Protein
chemical_list: D001426:Bacterial Proteins; D004259:DNA-Directed DNA Polymerase; D003854:Deoxyribonucleotides; D029968:Escherichia coli Proteins; D009701:Nucleoside-Diphosphate Kinase; D009709:Nucleotide Deaminases; D011938:Rec A Recombinases; D012293:Rifampin; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein; C078202:UmuC protein, E coli; C019988:dCTP deaminase
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