Published online 23 January 2004
Nucleic Acids Research, 2004, Vol. 32, No. 2 477-487
© 2004 Oxford University Press
Identification and characterization of two forms of mouse MUTYH proteins encoded by alternatively spliced transcripts
1 Division of Neurofunctional Genomics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Fukuoka 812–8582, Japan and 2 Division of Molecular and Cell Therapeutics, Department of Molecular Genetics, Medical Institute of Bioregulation, Kyushu University, Tsurumihara 4546, Beppu, Oita 874–0838, Japan
*To whom correspondence should be addressed. Tel: +81 92 642 6800; Fax: +81 92 642 6791; Email: yusaku{at}bioreg.kyushu-u.ac.jp
+AB117937–AB117939
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 (MUTYH
), while type c mRNA had a partly different open reading frame encoding a 50.2 kDa protein (MUTYHß). An in vitro translation of type b and c mRNAs produced a 50 kDa MUTYH and 47 kDa MUTYHß, respectively. MUTYH and MUTYHß 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 MUTYH and MUTYHß were mainly localized in the nuclei and some in mitochondria in wild-type ES cells. Recombinant MUTYH and ß were expressed as fusion proteins with thioredoxin in Escherichia coli, but only MUTYH was partly soluble and thus could be purified. Recombinant MUTYH possessed DNA glycosylase activities to excise adenine opposite 8-oxoguanine and guanine but not AP lyase activity.
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