Isolation and characterization of cDNA and genomic sequences for mouse O6-methylguanine-DNA methyltransferase

Akiko Shiraishi, Kunihiko Sakumi, Yoshimichi Nakatsu, Hiroshi Hayakawa, Mutsuo Sekiguchi

研究成果: ジャーナルへの寄稿記事

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An enzyme, O6-methylguanine-DNA methyltransferase, is present in various organisms and plays an important role in repair of DNA damaged by alkylating agents. The enzyme transfers methyl groups from O6-methylguanine and other methylated moieties of the DNA to its own molecule. As a first step to construct animal models with altered levels of the enzyme activity, we cloned cDNA and genomic DNA sequences for mouse methyltransferase and elucidated their structures. The nucleotide sequence of the cDNA revealed an open reading frame comprising 211 amino acid residues. The mol. wt of mouse O6-methylguanine-DNA methyltransferase, calculated from the predicted amino acid sequence, was 22 400, and the methyltransferase protein of this size was present when the cDNA was expressed in methyltransferasedeficient human cells. The predicted amino acid sequence of the mouse methyltransferase exhibits an intense homology with those of human and bacterial counterparts. Using the cDNA as a probe, part of the mouse gene for methyltransferase was isolated. The gene consisted of at least four exons and spanned > 145 KB. Sequences around the exon/intron junctions for the mouse gene are almost the same as those for the human species.

元の言語英語
ページ(範囲)289-296
ページ数8
ジャーナルCarcinogenesis
13
発行部数2
DOI
出版物ステータス出版済み - 2 1 1992

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All Science Journal Classification (ASJC) codes

  • Cancer Research

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