
The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein. The interaction between AlkB and RecA was validated by yeast two-hybrid assay; size-exclusion chromatography and standard pull down experiment and was shown to be direct and mediated by the N-terminal domain of RecA. RecA binding results AlkB-RecA heterodimer formation and RecA-AlkB repairs alkylated DNA with higher efficiency than AlkB alone.
Models, Molecular, DNA Repair, AlkB Enzymes, Molecular Conformation, Genome Integrity, Repair and Replication, DNA Methylation, DNA Adducts, Rec A Recombinases, Escherichia coli, Protein Interaction Domains and Motifs, Carrier Proteins, Oxidation-Reduction, Protein Binding
Models, Molecular, DNA Repair, AlkB Enzymes, Molecular Conformation, Genome Integrity, Repair and Replication, DNA Methylation, DNA Adducts, Rec A Recombinases, Escherichia coli, Protein Interaction Domains and Motifs, Carrier Proteins, Oxidation-Reduction, Protein Binding
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