Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-12-16
pubmed:abstractText
The mutational specificities of various chemical mutagens were compared in isogenic E. coli strains with different DNA repair capabilities (wild-type, uvrA, umuC, and uvrA umuC) in a reversion assay employing a set of mutant lacZ genes that can detect two types of transitions, four types of transversions, and five kinds of specific frameshift events. A uvrA derivative was more sensitive than the wild-type strain to 3-chloro-4-(dichloromethyl)-5-hydroxy-2(5H)-furanone for +1G, -1G, -2(C-G), +1A and -1A frameshifts, G.C-->A.T transitions, and G.C-->T.A transversions. In a uvrA background, G.C-->T.A transversions and +1G, +1A, and -1A frameshifts appeared to be umuC-dependent, while G.C-->A.T transitions were not. N-Ethyl-N'-nitro-N-nitrosoguanidine was more mutagenic in a uvrA background for five kinds of frameshifts and G.C-->A.T transitions, but not for G.C-->T.A, A.T-->C.G, and A.T-->G.C base substitutions. A.T-->C.G transversions were totally dependent on umuC gene function. For the investigation of mutational specificities induced by frameshift mutagens, an rfa mutation was additionally introduced. The rfa strain responded to 2-nitrofluorene, which induced primarily -2(C-G) frameshift mutations. In an rfa uvrA background, benzo[a]pyrene induced +1G, -1G, +1A, and -1A frameshifts. 2-Aminoanthracene induced +1G, -1G, and +1A, but not -1A, frameshifts, with -1G frameshifts predominating. Ethidium bromide induced only two types of frameshifts, -1G and +1A. Frameshifts induced by ICR-170 were independent of umuC gene function, while those by induced 1-nitropyrene were partly umuC-dependent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-nitropyrene, http://linkedlifedata.com/resource/pubmed/chemical/2-anthramine, http://linkedlifedata.com/resource/pubmed/chemical/2-nitrofluorene, http://linkedlifedata.com/resource/pubmed/chemical/3-chloro-4-(dichloromethyl)-5-hydrox..., http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Aminoacridines, http://linkedlifedata.com/resource/pubmed/chemical/Anthracenes, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Benzo(a)pyrene, http://linkedlifedata.com/resource/pubmed/chemical/DNA Ligases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase, http://linkedlifedata.com/resource/pubmed/chemical/ENNG, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ethidium, http://linkedlifedata.com/resource/pubmed/chemical/Fluorenes, http://linkedlifedata.com/resource/pubmed/chemical/Furans, http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Methotrexate, http://linkedlifedata.com/resource/pubmed/chemical/Methylnitronitrosoguanidine, http://linkedlifedata.com/resource/pubmed/chemical/Mutagens, http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Mustard Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Pyrenes, http://linkedlifedata.com/resource/pubmed/chemical/UmuC protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/UmuD protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/UvrA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/acridine mustard, http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase, http://linkedlifedata.com/resource/pubmed/chemical/lipooligosaccharide...
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-5107
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
311
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-304
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7526195-Adenosine Triphosphatases, pubmed-meshheading:7526195-Aminoacridines, pubmed-meshheading:7526195-Anthracenes, pubmed-meshheading:7526195-Bacterial Proteins, pubmed-meshheading:7526195-Benzo(a)pyrene, pubmed-meshheading:7526195-DNA Ligases, pubmed-meshheading:7526195-DNA Repair, pubmed-meshheading:7526195-DNA-Binding Proteins, pubmed-meshheading:7526195-DNA-Directed DNA Polymerase, pubmed-meshheading:7526195-Escherichia coli, pubmed-meshheading:7526195-Escherichia coli Proteins, pubmed-meshheading:7526195-Ethidium, pubmed-meshheading:7526195-Fluorenes, pubmed-meshheading:7526195-Frameshift Mutation, pubmed-meshheading:7526195-Furans, pubmed-meshheading:7526195-Genes, Bacterial, pubmed-meshheading:7526195-Glycosyltransferases, pubmed-meshheading:7526195-Lac Operon, pubmed-meshheading:7526195-Methotrexate, pubmed-meshheading:7526195-Methylnitronitrosoguanidine, pubmed-meshheading:7526195-Mutagenesis, pubmed-meshheading:7526195-Mutagenicity Tests, pubmed-meshheading:7526195-Mutagens, pubmed-meshheading:7526195-Nitrogen Mustard Compounds, pubmed-meshheading:7526195-Point Mutation, pubmed-meshheading:7526195-Pyrenes, pubmed-meshheading:7526195-Species Specificity, pubmed-meshheading:7526195-Suppression, Genetic, pubmed-meshheading:7526195-beta-Galactosidase
pubmed:year
1994
pubmed:articleTitle
Effects of DNA repair deficiency on the mutational specificity in the lacZ gene of Escherichia coli.
pubmed:affiliation
Laboratory of Genetic Toxicology, Institute of Environmental Toxicology, Tokyo, Japan.
pubmed:publicationType
Journal Article, Comparative Study