Abstract
The O6-alkylguanine DNA alkyltransferase (AGT) is a highly conserved protein responsible for direct repair of alkylated guanine and to a lesser degree thymine bases. While specific DNA lesion-bound complexes in crystal structures consist of monomeric AGT, several solution studies have suggested that cooperative DNA binding plays a role in the physiological activities of AGT. Cooperative AGT-DNA complexes have been described by theoretical models, which can be tested by atomic force microscopy (AFM). Direct access to structural features of AGT-DNA complexes at the single molecule level by AFM imaging revealed non-specifically bound, cooperative complexes with limited cluster length. Implications of cooperative binding in AGT-DNA interactions are discussed.
Original language | English |
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Pages (from-to) | 14-22 |
Number of pages | 9 |
Journal | DNA Repair |
Volume | 20 |
DOIs | |
State | Published - Aug 2014 |
Bibliographical note
Funding Information:This study was supported by the Deutsche Forschungsgemeinschaft (DFG, Forschungszentrum FZ82 to IT) and National Institutes of Health (NIH, GM-070662 to MGF).
Keywords
- Atomic force microscopy (AFM)
- Cooperative protein-DNA interactions
- DNA repair
- Single molecule imaging
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology