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Correlation between the Phosphohydrolase Activity of the Escherichia coli Orf135 (NudG) Protein and Mutation Suppression
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. |
(Relation)isversionof: | http://ci.nii.ac.jp/naid/110006279220/ |
Type: | article |
URI: | http://hdl.handle.net/2115/30114 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 紙谷 浩之
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