PMID: 11329883May 2, 2001Paper

2-hydroxyadenine in DNA is a very poor substrate of the Escherichia coli MutY protein

Journal of Radiation Research
H Kamiya, H Kasai

Abstract

To test the possibility that the Escherichia coli MutY or MutM protein acts as a 2-hydroxyadenine (2-OH-Ade) glycosylase, we treated double-stranded oligodeoxyribonucleotides containing 2-OH-Ade with the E. coli MutY or MutM protein in vitro. We found that a strand with 2-OH-Ade was a very poor substrate of MutY, irrespective of the base in the complementary strand. Moreover, a strand containing adenine or guanine opposite 2-OH-Ade was also rarely cleaved by MutY. The cleavage of oligonucleotides with 2-OH-Ade by MutM was not observed. These results indicate that neither MutY nor MutM plays an important role in the removal of 2-OH-Ade from DNA.

References

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Jun 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·J TchouS Nishimura
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Jul 17, 1999·Journal of Radiation Research·S Yanase, N Ishi

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Citations

Apr 16, 2014·Scientific Reports·Mizuki OhnoYusaku Nakabeppu

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