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

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タイトル: Correlation between the Phosphohydrolase Activity of the Escherichia coli Orf135 (NudG) Protein and Mutation Suppression
著者: Kamiya, Hiroyuki 著作を一覧する
Iida, Emiko 著作を一覧する
Harashima, Hideyoshi 著作を一覧する
キーワード: Orf135
phosphohydrolase activity
mutation suppression
nucleotide pool sanitization
発行日: 2007年 5月28日
出版者: The Environmental Mutagen Society of Japan
誌名: Genes and environment : the official journal of the Japanese Environmental Mutagen Society
巻: 29
号: 2
開始ページ: 63
終了ページ: 66
出版社 DOI: 10.3123/jemsge.29.63
抄録: 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.
資料タイプ: article
URI: http://hdl.handle.net/2115/30114
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 紙谷 浩之

 

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