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PMID: 15380096 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Alkylation damage in DNA and RNA--repair mechanisms and medical significance.

DNA repair ·Vol. 3 ·No. 11 ·2004-11-02 ·Pages 1389-407

Drabløs F, Feyzi E, Aas PA, Vaagbø CB, Kavli B, Bratlie MS, Peña-Diaz J, Otterlei M, Slupphaug G, Krokan HE

Abstract

Alkylation lesions in DNA and RNA result from endogenous compounds, environmental agents and alkylating drugs. Simple methylating agents, e.g. methylnitrosourea, tobacco-specific nitrosamines and drugs like temozolomide or streptozotocin, form adducts at N- and O-atoms in DNA bases. These lesions are mainly repaired by direct base repair, base excision repair, and to some extent by nucleotide excision repair (NER). The identified carcinogenicity of O(6)-methylguanine (O(6)-meG) is largely caused by its miscoding properties. Mutations from this lesion are prevented by O(6)-alkylG-DNA alkyltransferase (MGMT or AGT) that repairs the base in one step. However, the genotoxicity and cytotoxicity of O(6)-meG is mainly due to recognition of O(6)-meG/T (or C) mispairs by the mismatch repair system (MMR) and induction of futile repair cycles, eventually resulting in cytotoxic double-strand breaks. Therefore, inactivation of the MMR system in an AGT-defective background causes resistance to the killing effects of O(6)-alkylating agents, but not to the mutagenic effect. Bifunctional alkylating agents, such as chlorambucil or carmustine (BCNU), are commonly used anti-cancer drugs. DNA lesions caused by these agents are complex and require complex repair mechanisms. Thus, primary chloroethyl adducts at O(6)-G are repaired by AGT, while the secondary highly cytotoxic interstrand cross-links (ICLs) require nucleotide excision repair factors (e.g. XPF-ERCC1) for incision and homologous recombination to complete repair. Recently, Escherichia coli protein AlkB and human homologues were shown to be oxidative demethylases that repair cytotoxic 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) residues. Numerous AlkB homologues are found in viruses, bacteria and eukaryotes, including eight human homologues (hABH1-8). These have distinct locations in subcellular compartments and their functions are only starting to become understood. Surprisingly, AlkB and hABH3 also repair RNA. An evaluation of the biological effects of environmental mutagens, as well as understanding the mechanism of action and resistance to alkylating drugs require a detailed understanding of DNA repair processes.

MeSH Terms
AlkB Homolog 1, Histone H2a Dioxygenase Alkylating Agents/metabolism,toxicity Alkylation Amino Acid Sequence Animals Carcinogens/metabolism,toxicity DNA/chemistry,metabolism DNA Damage DNA Repair DNA Repair Enzymes/genetics,metabolism Escherichia coli Proteins/genetics,metabolism Humans Mixed Function Oxygenases/genetics,metabolism Models, Biological Molecular Sequence Data Neoplasms/drug therapy,metabolism Phylogeny RNA/chemistry,metabolism Sequence Homology, Amino Acid
Chemicals
Alkylating Agents Carcinogens Escherichia coli Proteins RNA DNA Mixed Function Oxygenases AlkB protein, E coli ALKBH1 protein, human AlkB Homolog 1, Histone H2a Dioxygenase DNA Repair Enzymes
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Drabløs Finn
Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, N-7489 Trondheim, Norway.
Feyzi Emadoldin
Aas Per Arne
Vaagbø Cathrine B
Kavli Bodil
Bratlie Marit S
Peña-Diaz Javier
Otterlei Marit
Slupphaug Geir
Krokan Hans E
Article Info
Journal
DNA repair
Abbr.
DNA Repair (Amst)
ISSN
1568-7864
Published
2004-11-02
Pages
1389-407
Language
English
Region
Netherlands
NLM ID
101139138
Subset
IM
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