DNA glycosylase recognition and catalysis

Curr Opin Struct Biol. 2004 Feb;14(1):43-9. doi: 10.1016/j.sbi.2004.01.003.

Abstract

DNA glycosylases are the enzymes responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Recent structural and biochemical results have provided novel insights into DNA damage recognition and repair. The basis of the recognition of the oxidative lesion 8-oxoguanine by two structurally unrelated DNA glycosylases is now understood and has been revealed to involve surprisingly similar strategies. Work on MutM (Fpg) has produced structures representing three discrete reaction steps. The NMR structure of 3-methyladenine glycosylase I revealed its place among the structural families of DNA glycosylases and the X-ray structure of SMUG1 likewise confirmed that this protein is a member of the uracil DNA glycosylase superfamily. A novel disulfide cross-linking strategy was used to obtain the long-anticipated structure of MutY bound to DNA containing an A*oxoG mispair.

Publication types

  • Review

MeSH terms

  • Catalysis
  • DNA / metabolism*
  • DNA Glycosylases / chemistry*
  • DNA Glycosylases / metabolism*
  • DNA Repair*
  • DNA-Formamidopyrimidine Glycosylase / metabolism*
  • Guanine / analogs & derivatives*
  • Guanine / metabolism
  • Models, Molecular
  • Structure-Activity Relationship
  • Uracil-DNA Glycosidase

Substances

  • 8-hydroxyguanine
  • Guanine
  • DNA
  • 3-methyladenine-DNA glycosylase
  • DNA Glycosylases
  • Uracil-DNA Glycosidase
  • mutY adenine glycosylase
  • DNA-Formamidopyrimidine Glycosylase