XPG protein has a structure-specific endonuclease activity

  • Mutat Res. 1995 Jul;347(2):55-60. doi: 10.1016/0165-7992(95)90070-5.
K G Cloud  1 ,  B Shen ,  G F Strniste ,  M S Park
Affiliations
  • 1. Life Sciences Division, Los Alamos National Laboratory, NM 87545, USA.
PMID: 7651464 DOI: 10.1016/0165-7992(95)90070-5
Abstract

Biochemically active human DNA repair protein, xeroderma pigmentosum G (XPG), was overexpressed in insect cells by a Recombinant baculovirus. The Recombinant baculovirus produced XPG with a mobility of approximately 185 kDa in a denaturing polyacrylamide gel. Indirect immunofluorescence studies demonstrated that the Recombinant full-length XPG protein was expressed predominantly as a nuclear protein. The Recombinant XPG protein was purified to apparent homogeneity using Q-sepharose, S-300 size exclusion, and Mono Q column chromatography. XPG protein showed a structure-specific DNA Endonuclease activity, and a preferential affinity to single-stranded DNA and RNA compared to double-stranded DNA.