A conserved 5' to 3' exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG

J Biol Chem. 1994 Dec 16;269(50):31342-5.

Abstract

Saccharomyces cerevisiae RAD2 protein and its human homolog xeroderma pigmentosum group G (XPG) protein function in the incision step of nucleotide excision repair of DNA damaged by ultraviolet light. Both RAD2 and XPG proteins have been shown previously to possess an endonuclease activity. Using DNA substrates labeled at either the 5' end or 3' end, we now demonstrate that RAD2 protein also digests both single-stranded and double-stranded DNAs exonucleolytically with a 5' to 3' directionality. A 5' to 3' exonuclease activity is also present in the XPG protein, indicating evolutionary conservation of this activity. The possible role of RAD2 and XPG 5' to 3' exonuclease activity in nucleotide excision repair is discussed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • DNA Repair*
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases*
  • Endonucleases
  • Exonucleases / metabolism*
  • Fungal Proteins / metabolism*
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins
  • Oligodeoxyribonucleotides / chemistry
  • Recombinant Proteins
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors
  • Xeroderma Pigmentosum / enzymology

Substances

  • DNA excision repair protein ERCC-5
  • DNA-Binding Proteins
  • Fungal Proteins
  • Nuclear Proteins
  • Oligodeoxyribonucleotides
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • RAD2 protein, S cerevisiae
  • Endodeoxyribonucleases
  • Endonucleases
  • Exonucleases