Source:http://linkedlifedata.com/resource/pubmed/id/11506801
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| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2001-8-16
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| pubmed:abstractText |
MMS, an S(N)2 alkylating agent, is a moderate inducer of SOS mutagenesis and adaptive response. Our previous studies have shown that transient starvation of Escherichia coli AB1157argE3 strain causes a decrease of MMS-induced argE3-->Arg(+) reversions and this decrease is accompanied by the disappearance of the Fpg protein sensitive sites on plasmids isolated from MMS-treated and subsequently starved bacteria. This suggests that in such cells the mutation frequency decline (MFD) repair takes place. Here, we study the relation between MMS-induced mutagenesis as well as mutation frequency decline during starvation, and the repair of alkylated bases and AP-sites by base and nucleotide excision repair systems. In the AB1157alkA(-) strain, MMS-induced mutagenesis was over five-fold higher than in the wild type strain and no MFD repair occurred during starvation. Surprisingly, the lack of TagA glycosylase diminished MMS mutagenesis and accelerated the MFD effect. However, in double tagA(-)alkA(-) mutant, the frequency of Arg(+) reversions increased over 10-fold during 60 min of aminoacid starvation after MMS-treatment. Lack of the uvrA gene function did not affect the MMS-induced mutation rate and MFD in AB1157alkA(+)tagA(+). Starvation of MMS treated AB1157tagAalkAuvrA triple mutant caused a decrease of mutation frequency almost to the level of spontaneous mutation rate. Examination of the repair of 3-MeAde, 7-MeGua and AP sites during starvation using repair glycosylases and plasmids isolated from MMS-treated and starved bacteria revealed that in E. coli uvr(+) but tagAalkA strain, neither 3-MeAde nor 7-MeGua were repaired during 60 min starvation and these persistent lesions could be responsible for the induction of the SOS system and an increase in mutation rate during starvation. In the triple tagAalkAuvrA mutant the repair of 3-MeAde, 7-MeGua and AP sites was carried out effectively and this could explain the observed decrease in the mutation rate during starvation. These results suggest that only in the absence of the "first choice" repair enzymes TagA, AlkA glycosylases and UvrABC excinuclease, a third error-free repair system of alkylated bases is activated. In the absence of only TagA and AlkA glycosylases, UvrABC excinuclease mediates activation of the SOS response, and this results in an increase of mutagenesis induced by the presence of alkylated bases in DNA.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Oxygen Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-(Apurinic or Apyrimidinic...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-3-methyladenine glycosidase II,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease IV (Phage...,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methyl Methanesulfonate,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/TagA protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/endodeoxyribonuclease uvrABC,
http://linkedlifedata.com/resource/pubmed/chemical/endonuclease IV, E coli
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0027-5107
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
480-481
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
77-84
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11506801-Bacterial Proteins,
pubmed-meshheading:11506801-Carbon-Oxygen Lyases,
pubmed-meshheading:11506801-DNA, Bacterial,
pubmed-meshheading:11506801-DNA Glycosylases,
pubmed-meshheading:11506801-DNA Ligases,
pubmed-meshheading:11506801-DNA Repair,
pubmed-meshheading:11506801-DNA-(Apurinic or Apyrimidinic Site) Lyase,
pubmed-meshheading:11506801-Deoxyribonuclease IV (Phage T4-Induced),
pubmed-meshheading:11506801-Endodeoxyribonucleases,
pubmed-meshheading:11506801-Escherichia coli,
pubmed-meshheading:11506801-Escherichia coli Proteins,
pubmed-meshheading:11506801-Lipoproteins,
pubmed-meshheading:11506801-Methyl Methanesulfonate,
pubmed-meshheading:11506801-Models, Biological,
pubmed-meshheading:11506801-Mutagenesis,
pubmed-meshheading:11506801-Mutagenicity Tests,
pubmed-meshheading:11506801-N-Glycosyl Hydrolases,
pubmed-meshheading:11506801-Plasmids
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| pubmed:year |
2001
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| pubmed:articleTitle |
Contribution of E. coli AlkA, TagA glycosylases and UvrABC-excinuclease in MMS mutagenesis.
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| pubmed:affiliation |
Department of Molecular Biology, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul. Pawiñskiego 5A, 02-106 Warszawa, Poland. elag@ibb.waw.pl
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| pubmed:publicationType |
Journal Article
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