open access

https://hdl.handle.net/2115/30114

Correlation between the Phosphohydrolase Activity of the Escherichia coli Orf135 (NudG) Protein and Mutation Suppression

英語

nucleotide pool sanitization

2007-05-28

The Environmental Mutagen Society of Japan

Genes and environment : the official journal of the Japanese Environmental Mutagen Society

29(2)

63-66

The Escherichia coli Orf135 (NudG) protein, a MutT-type enzyme, catalyzes the hydrolysis of 2-hydroxy-dATP and 8-hydroxy-dGTP, and its deficiency causes an increase in the mutation frequency. In this study, Orf135 proteins with substitutions at the Gly-36, Gly-37, Lys-38, Glu-43, Arg-51, Glu-52, Leu-53, Glu-55, and Glu-56 residues, which are conserved in three MutT-type proteins (Orf135, MutT, and MTH1), were each expressed in the orf135- strain, and the rpoB mutant frequency upon H2O2 treatment was examined. The in vivo mutation suppression abilities and the in vitro enzymatic activities obtained in a previous study were compared. The expression of the enzymatically active Orf135 mutants in the orf135- strain tended to reduce the rpoB mutant frequency induced by H2O2. This result suggests the importance of the phosphohydrolase activity in the suppression of mutations by the Orf135 protein.

学術雑誌論文

Version of Record

日本環境変異原学会. 本文データは日本環境変異原学会の許諾に基づきCiNiiから複製したものである.

1880-7046

1880-7062