XPG protein has a structure-specific endonuclease activity.

K G Cloud; B Shen; G F Strniste; M S Park

doi:10.1016/0165-7992(95)90070-5

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XPG protein has a structure-specific endonuclease activity.

K G Cloud·B Shen·G F Strniste·M S Park

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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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Animals Base Sequence Cells, Cultured DNA Repair DNA-Binding Proteins Endonucleases Genetic Vectors Microscopy, Fluorescence Molecular Sequence Data Nuclear Proteins Spodoptera Transcription Factors Xeroderma Pigmentosum DNA Excision Repair Protein ERCC-5 Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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K G Cloud, B Shen, G F Strniste, M S Park. 1995. XPG protein has a structure-specific endonuclease activity.. https://doi.org/10.1016/0165-7992(95)90070-5

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