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. 1995 Jul;347(2):55-60.
doi: 10.1016/0165-7992(95)90070-5.

XPG protein has a structure-specific endonuclease activity

K G Cloud  1 , B Shen, G F Strniste, M S Park
Affiliations

XPG protein has a structure-specific endonuclease activity

K G Cloud et al. Mutat Res. 1995 Jul.

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.

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