Detail of "3373-53-3"

Reference

Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein

Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein. Hashiguchi, K.; Zhang, Q. M.; Sugiyama, H.; Ikeda, S.; Yonei, S. ( Laboratory of Radiation Biology, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan). International Journal of Radiation Biology, 78(7), 585-592 (English) 2002 Taylor & Francis Ltd. CODEN: IJRBE7. ISSN: 0955-3002. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 7 Purpose: 2-Hydroxyadenine (2-ohA) is an oxidn. product of adenine generated in DNA by ionizing radiation and various chem. oxidants. 2-OhA has mutational potential comparable to that of 8-oxoguanine in bacteria and mammalian cells. Recent studies have shown that 2-ohA is removed from DNA by a human MutY homolog, MYH protein, in vitro. On the other hand, the repair mechanisms for 2-ohA in Escherichia coli are not yet understood. Materials and methods: Gel shift assays were used to assess the binding activity of E. coli full-length MutY protein and its N-terminal (residues 1-226) domain (M25) to 2-ohA/G-, 2-ohA/A-, 2-ohA/C- and 2-ohA/T-contg. 24-mer oligonucleotides. Furthermore, whether these proteins specifically cleave 2-ohA-contg. duplex oligonucleotides was examd. Results: The purified MutY and M25 proteins had similar binding affinities to 2-ohA/G-, 2-ohA/A- and 2-ohA/C-contg. oligonucleotides. MutY protein removed 2-ohA preferentially from 2-ohA/G mispairs. M25 protein showed the reduced catalytic activity for 2-ohA/G-contg. oligonucleotides. Conclusions: E. coli MutY protein has a DNA glycosylase activity that removes 2-ohA from 2-ohA/G mispairs in DNA. The C-terminal domain is required for the removal of 2-ohA from DNA, but is not crucial for binding to 2-ohA-contg. 124834-14-6 and 3373-53-3 are just another two chemicals used in this study. oligonucleotides. .

Oxidative DNA lesions and mutagenesis

Oxidative DNA lesions and mutagenesis. Kamiya, Hiroyuki; Kasai, Hiroshi (Dep. Environmental Oncol., Univ. Occupational Environmental Health, Kitakyushu 807, Japan). Kankyo Hen'igen Kenkyu, Volume Date 1996, 18(3), 181-189 (Japanese) 1997 Nippon Kankyo Hen'igen Gakkai. CODEN: KHKEEN. ISSN: 0910-0865. DOCUMENT TYPE: Journal; General Review CA Section: 4 (Toxicology) A review and discussion with many refs. 3373-53-3 and 5614-64-2 are cas registry numbers of chemicals which are used as reagents here. on the mutational properties of oxidative DNA lesions, particularly those of 8-hydroxyguanine and 2-hydroxyadenine. DNA lesions produced by reactive oxygen appears to be one of the causes of mutation that either occurs spontaneously or is induced by environmental mutagens. 8-Hydroxyguanine has been studied extensively and it has been shown that the base induces G?T transversion. Recent studies indicate that another oxidative DNA lesion, 2-hydroxyadenine, also induces mutation. .