Insight into the cooperative DNA binding of the O6-alkylguanine DNA alkyltransferase

Ingrid Tessmer, Michael G. Fried

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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 languageEnglish
Pages (from-to)14-22
Number of pages9
JournalDNA Repair
Volume20
DOIs
StatePublished - 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

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