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Abstracts
The Escherichia coli AlkB protein encoded by alkB gene was recently found to repair cytotoxic DNA lesions 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) by using a novel iron-catalysed oxidative demethylation mechanism that protects the cell from the toxic effects of methylating agents. Mutation in alkB results in increased sensitivity to MMS and elevated level of MMS-induced mutations. The aim of this study was to analyse the mutational specificity of alkB117 in a system developed by J.H. Miller involving two sets of E. coli lacZ mutants, CC101-106 allowing the identification of base pair substitutions, and CC107-CC111 indicating frameshift mutations. Of the six possible base substitutions, the presence of alkB117 allele led to an increased level of GC→AT transitions and GC→TA and AT→TA transversions. After MMS treatment the level of GC→AT transitions increased the most, 22-fold. Among frameshift mutations, the most numerous were -2CG, -1G, and -1A deletions and +1G insertion. MMS treatment appreciably increased all of the above types of frameshifts, with additional appearance of the +1A insertion.
Journal
Year
Volume
Issue
Pages
425-428
Physical description
Dates
published
2006
received
2006-02-16
revised
2006-03-17
accepted
2006-05-05
(unknown)
2006-05-29
Contributors
author
- Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
author
- Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
author
- Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv53p425kz