イチノエ　アキマサ   Ichinoe Akimasa   一戸　晶元    所属   医学部 医学科（附属足立医療センター）    職種   講師
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	Identification and characterization of two forms of mouse MUTYH proteins encoded by alternatively spliced transcripts.
掲載誌名	正式名：Nucleic acids research 略　 称：Nucleic Acids Res ISSNコード：03051048/13624962
掲載区分	国外
巻・号・頁	32(2),pp.477-487
総ページ数	11
著者・共著者	Akimasa Ichinoe†, Behmanesh Mehrdad, Yohei Tominaga, Yasuhiro Ushijima, Seiki Hirano, Yasunari Sakai, Daisuke Tsuchimoto, Kunihiko Sakumi, Norio Wake, Yusaku Nakabeppu
担当区分	筆頭著者
発行年月	2004/01/23
概要	There are three types of mouse Mutyh mRNAs (type a, b and c) generated by alternative splicing, and type b mRNA is a major form among the three in most of the tissues examined. The level of type c mRNA is relatively high in brain. Type a and b mRNAs were expected to encode 57.7 kDa protein (MUTYHalpha), while type c mRNA had a partly different open reading frame encoding a 50.2 kDa protein (MUTYHbeta). An in vitro translation of type b and c mRNAs produced a 50 kDa MUTYHalpha and 47 kDa MUTYHbeta, respectively. MUTYHalpha and MUTYHbeta were detected in wild-type embryonic stem (ES) cells or thymocytes prepared from wild-type mice, but neither MUTYH-null ES cells nor thymocytes prepared from MUTYH-null mice. Both MUTYHalpha and MUTYHbeta were mainly localized in the nuclei and some in mitochondria in wild-type ES cells. Recombinant MUTYHalpha and beta were expressed as fusion proteins with thioredoxin in Escherichia coli, but only MUTYHalpha was partly soluble and thus could be purified. Recombinant MUTYHalpha possessed DNA glycosylase activities to excise adenine opposite 8-oxoguanine and guanine but not AP lyase activity.
DOI	10.1093/nar/gkh214