Nucleic Acids Research, 2000, Vol. 28, No. 6 1355-1364
© 2000 Oxford University Press
Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria
1Department of Biochemistry, Medical Institute of Bioregulation and 2Department of Medicine and Clinical Science, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan, 3Biomolecular Engineering Research Institute, Osaka 565-0874, Japan, 4Department of Biology, Fukuoka Dental College, Fukuoka 814-0175, Japan, 5Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka 814-0180, Japan and 6CREST, Japan Science and Technology Corporation, Japan
An enzyme activity introducing an alkali-labile site at 2-hydroxyadenine (2-OH-A) in double-stranded oligonucleotides was detected in nuclear extracts of Jurkat cells. This activity co-eluted with activities toward adenine paired with guanine and 8-oxo-7,8-dihydroguanine (8-oxoG) as a single peak corresponding to a 55 kDa molecular mass on gel filtration chromatography. Further co-purification was then done. Western blotting revealed that these activities also co-purified with a 52 kDa polypeptide which reacted with antibodies against human MYH (anti-hMYH). Recombinant hMYH has essentially similar activities to the partially purified enzyme. Thus, hMYH is likely to possess both adenine and 2-OH-A DNA glycosylase activities. In nuclear extracts from Jurkat cells, a 52 kDa polypeptide was detected with a small amount of 53 kDa polypeptide, while in mitochondrial extracts a 57 kDa polypeptide was detected using anti-hMYH. With amplification of the 5'-regions of the hMYH cDNA, 10 forms of hMYH transcripts were identified and subgrouped into three types, each with a unique 5' sequence. These hMYH transcripts are likely to encode multiple authentic hMYH polypeptides including the 52, 53 and 57 kDa polypeptides detected in Jurkat cells.
* To whom correspondence should be addressed at: Department of Biochemistry, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Muidushi, Higashi-ku, Fukuoka 812-8582, Japan. Tel: +81 92 642 6800; Fax: +81 92 642 6791; Email: yusaku@bioreg.kyushu-u.ac.jpPresent address:Hisanobu Oda, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto 862-0976, Japan, Yasuyuki Imaiso, deceased (July 18, 1999)
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