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

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Title: Correlation between the Phosphohydrolase Activity of the Escherichia coli Orf135 (NudG) Protein and Mutation Suppression
Authors: Kamiya, Hiroyuki Browse this author
Iida, Emiko Browse this author
Harashima, Hideyoshi Browse this author →KAKEN DB
Keywords: Orf135
phosphohydrolase activity
mutation suppression
nucleotide pool sanitization
Issue Date: 28-May-2007
Publisher: The Environmental Mutagen Society of Japan
Journal Title: Genes and environment : the official journal of the Japanese Environmental Mutagen Society
Volume: 29
Issue: 2
Start Page: 63
End Page: 66
Publisher DOI: 10.3123/jemsge.29.63
Abstract: 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.
Rights: 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.
Type: article
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 紙谷 浩之

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