Plant Molecular Biology

, Volume 47, Issue 6, pp 795–804

An OGG1 orthologue encoding a functional 8-oxoguanine DNA glycosylase/lyase in Arabidopsis thaliana

  • Maria-Victoria García-Ortiz
  • Rafael R. Ariza
  • Teresa Roldán-Arjona
Article

DOI: 10.1023/A:1013644026132

Cite this article as:
García-Ortiz, MV., Ariza, R.R. & Roldán-Arjona, T. Plant Mol Biol (2001) 47: 795. doi:10.1023/A:1013644026132

Abstract

Repair of the ubiquitous mutagenic lesion 7,8-dihydro-8-oxoguanine (8-oxoG) is initiated in eukaryotes by DNA glycosylases/lyases, such as yeast Ogg1, that do not share significant sequence identity with their prokaryotic counterparts, typified by Escherichia coli MutM (Fpg) protein. The unexpected presence of a functional mutM orthologue in the model plant Arabidopsis thaliana has brought into question the existence of functional OGG1 orthologues in plants. We report here the cDNA cloning, expression and functional characterization of AtOGG1, an Arabidopsisthaliana gene widely expressed in different plant tissues which encodes a 40.3 kDa protein with significant sequence identity to yeast and human Ogg1 proteins. Purified AtOgg1 enzyme specifically cleaves duplex DNA containing an 8-OxoG:C mispair, and the repair reaction proceeds through an imine intermediate characteristic of all bifunctional DNA glycosylases/lyases. Consistent with its in vitro activity, expression of AtOGG1 suppresses the mutator phenotype of an E. coli strain deficient in 8-oxoG repair. Our results suggest that AtOgg1 is an structural and functional homologue of Ogg1 and establish the presence of two distinct 8-oxoG repair enzymes in Arabidopsis.

Arabidopsisthaliana 7,8-dihydro-8-oxoguanine DNA repair DNA glycosylase/lyase mutagenesis reactive oxygen species 

Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • Maria-Victoria García-Ortiz
    • 1
  • Rafael R. Ariza
    • 1
  • Teresa Roldán-Arjona
    • 1
  1. 1.Departamento de Genética, Facultad de CienciasUniversidad de CórdobaCórdobaSpain