XPG protein has a structure-specific endonuclease activity

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 ∼ 185 kDa in a denaturing polyacrylamide gel. Indirect immunofluorescence studies demonstrated tha...

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Bibliographic Details
Published in:Mutation research. Mutation research letters 1995-07, Vol.347 (2), p.55-60
Main Authors: Cloud, Kieran G., Shen, Binghui, Strniste, Gary F., Park, Min S.
Format: Article
Language:English
Subjects:
Baculovirus expression system
Biological and medical sciences
DNA repair
Fundamental and applied biological sciences. Psychology
Immunofluorescence, flap endonuclease
Molecular and cellular biology
Molecular genetics
Mutagenesis. Repair
Nuclear protein
Xeroderma pigmentosum group G
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Summary: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 ∼ 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.
ISSN:0165-7992
DOI:10.1016/0165-7992(95)90070-5