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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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 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.[1]

References

  1. XPG protein has a structure-specific endonuclease activity. Cloud, K.G., Shen, B., Strniste, G.F., Park, M.S. Mutat. Res. (1995) [Pubmed]
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