Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage

Biochemistry
B KarahalilM Dizdaroglu

Abstract

A gene from Schizosaccharomyces pombe, which encodes a protein with a strong sequence similarity to the Nth protein of Escherichia coli, has recently been identified [Roldán-Arjona, T., Anselmino, C., and Lindahl, T. (1996) Nucleic Acids Res. 24, 3307-3312]. The functional analysis of this eukaryotic enzyme indicated that it is a homologue of E. coli Nth protein. The gene has been subcloned and the protein (Nth-Spo) purified to apparent homogeneity. We investigated the substrate specificity of this eukaryotic enzyme for modified bases in oxidatively damaged DNA, using the technique of gas chromatography/isotope-dilution mass spectrometry (GC/IDMS). DNA substrates containing up to 17 types of modified bases were prepared by gamma-irradiation or by treatment with H2O2 in the presence of Fe(III)-EDTA or Cu(II). The results revealed an efficient excision of five pyrimidine-derived lesions, 5-hydroxycytosine, thymine glycol, 5-hydroxy-6-hydrothymine, 5,6-dihydroxycytosine, and 5-hydroxyuracil. None of the other pyrimidine or purine lesions was excised. Excision was measured as a function of enzyme concentration, time, substrate concentration, and temperature. Kinetic constants were determined. Although some DNA base lesions removed ...Continue Reading

References

Sep 1, 1990·International Journal of Radiation Biology·A F FuciarelliM Dizdaroglu
Nov 1, 1994·International Journal of Radiation Biology·S S Wallace
Jan 1, 1996·Annual Review of Biochemistry·A Sancar

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Citations

Nov 26, 2003·Mutation Research·Svein Bjelland, Erling Seeberg
Aug 1, 2000·Mutation Research·A Memisoglu, L Samson
Mar 29, 2001·Free Radical Biology & Medicine·M MurataS Kawanishi
Jun 28, 2002·Free Radical Biology & Medicine·Susan S Wallace
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Aug 13, 2005·The Journal of Biological Chemistry·Takashi WatanabeJeffrey P Bond
Apr 1, 2021·International Journal of Radiation Biology·Susan S Wallace

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