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[Chemically methylated DNA repair in Escherichia coli--the role of alkB protein].
- Source :
-
Postepy biochemii [Postepy Biochem] 2006; Vol. 52 (3), pp. 239-46. - Publication Year :
- 2006
-
Abstract
- Methylating agents belong to mutagens occurring most frequently in our environment. They methylate mainly the nitrogen bases in DNA and RNA, affecting their functions. In E. coli the alkylated bases are repaired by proteins and enzymes either permanently present in the cells (Ogt, Ada) or produced transiently (Ada, AlkB, AlkA, Aid), after induction of the Ada defence system. Alkylating agents induce also the SOS system, which enhances the synthesis of about 40 proteins, including those participating in recombination, replication and mutagenesis of DNA. All DNA interactions, modifications and repairs constitute an amazing and highly efficiently functioning cellular system. Among the repair proteins there are some which affect the alkylated bases in a non-conventional way, very rarely occurring in nature. Especially amazing is the mechanism of action of dioxogenase AlkB, which combines the repair of methyl-, ethyl- and etheno-base derivatives with oxidation and dissociation of the modified groups, leading to direct recovery of natural bases. This review attempts to elucidate the role of the individual proteins involved in the repair processes.
- Subjects :
- Alkylating Agents chemistry
DNA Glycosylases metabolism
DNA Repair Enzymes metabolism
DNA, Bacterial chemistry
DNA, Bacterial drug effects
DNA, Bacterial metabolism
Escherichia coli enzymology
Methylnitronitrosoguanidine chemistry
Methylnitrosourea chemistry
O(6)-Methylguanine-DNA Methyltransferase metabolism
SOS Response, Genetics
Transcription Factors metabolism
Alkylating Agents toxicity
DNA Damage
DNA Methylation drug effects
DNA Repair
Escherichia coli genetics
Escherichia coli Proteins metabolism
Mixed Function Oxygenases metabolism
Mutagens toxicity
Subjects
Details
- Language :
- Polish
- ISSN :
- 0032-5422
- Volume :
- 52
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Postepy biochemii
- Publication Type :
- Academic Journal
- Accession number :
- 17201058