Suppression of spontaneous and hydrogen peroxide-induced mutations by a MutT-type nucleotide pool sanitization enzyme, the Escherichia coli Orf135 protein

被引:37
作者
Kamiya, H
Iida, E
Murata-Kamiya, N
Yamamoto, Y
Miki, T
Harashima, H
机构
[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Kita Ku, Sapporo, Hokkaido 0600812, Japan
[2] Hokkaido Univ, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan
[3] Hyogo Med Univ, Nishinomiya, Hyogo 6638501, Japan
[4] Fukuoka Dent Coll, Sawara Ku, Fukuoka 8140193, Japan
关键词
D O I
10.1046/j.1365-2443.2003.00688.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Background: We recently found that the Escherichia coli Orf135 protein, a MutT-type enzyme, hydrolysed 2-hydroxy-dATP (2-OH-dATP), and less efficiently, 8-hydroxy-dGTP. Results: In this study, we examined the effects of the absence of the orf135 gene. Frequencies of spontaneous and H2O2-induced mutations were two- to three-fold higher in the orf135(-) strain than in the wild-type strain. These mutations include various mutations involving a G:C-->T:A transversion, the same type of mutation elicited by 2-OH-dATP. Over-expression of the Orf135 protein suppressed mutations even in the wild-type strain, as well as in the orf135(-) strain. Conclusions: The mutator phenotype of bacteria lacking the Orf135 protein suggests that this protein is involved in the suppression of mutations induced by oxidized deoxynucleotides in vivo and that various MutT-type enzymes contribute to nucleotide pool sanitization.
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页码:941 / 950
页数:10
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