Resolving the subtle details of human DNA alkyltransferase lesion search and repair mechanism by single-molecule studies

Proc Natl Acad Sci U S A. 2022 Mar 15;119(11):e2116218119. doi: 10.1073/pnas.2116218119. Epub 2022 Mar 8.

Abstract

SignificanceWe directly visualize DNA translocation and lesion recognition by the O6-alkylguanine DNA alkyltransferase (AGT). Our data show bidirectional movement of AGT monomers and clusters on undamaged DNA that depended on Zn2+ occupancy of AGT. A role of cooperative AGT clusters in enhancing lesion search efficiencies by AGT has previously been proposed. Surprisingly, our data show no enhancement of DNA translocation speed by AGT cluster formation, suggesting that AGT clusters may serve a different role in AGT function. Our data support preferential cluster formation by AGT at alkyl lesions, suggesting a role of these clusters in stabilizing lesion-bound complexes. From our data, we derive a new model for the lesion search and repair mechanism of AGT.

Keywords: DNA alkyltransferase; DNA repair; fluorescence optical tweezers; single-molecule studies.

MeSH terms

  • Alkyl and Aryl Transferases / chemistry*
  • Alkyl and Aryl Transferases / metabolism*
  • DNA / chemistry*
  • DNA / genetics*
  • DNA / metabolism
  • DNA Repair*
  • DNA, Single-Stranded
  • Humans
  • Ions
  • Models, Molecular
  • O(6)-Methylguanine-DNA Methyltransferase / chemistry
  • O(6)-Methylguanine-DNA Methyltransferase / metabolism
  • Protein Multimerization
  • Single Molecule Imaging* / methods
  • Structure-Activity Relationship
  • Zinc / chemistry

Substances

  • DNA, Single-Stranded
  • Ions
  • DNA
  • O(6)-Methylguanine-DNA Methyltransferase
  • Alkyl and Aryl Transferases
  • DNA alkyltransferase
  • Zinc