Fluorescence in situ hybridization mapping of the α and β subunits (HADHA and HADHB) of human mitochondrial fatty acid β-oxidation multienzyme complex to 2p23 and their evolution

被引:10
作者
Aoyama, T
Wakui, K
Orii, KE
Hashimoto, T
Fukushima, Y
机构
[1] Shinshu Univ, Sch Med, Dept Biochem, Matsumoto, Nagano 390, Japan
[2] Shinshu Univ, Sch Med, Dept Hyg & Med Genet, Matsumoto, Nagano 390, Japan
[3] Gifu Univ, Sch Med, Dept Pediat, Gifu 500, Japan
来源
CYTOGENETICS AND CELL GENETICS | 1997年 / 79卷 / 3-4期
关键词
D O I
10.1159/000134727
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Mitochondrial fatty acid beta-oxidation multienzyme complex/trifunctional protein has an alpha 4 beta 4 structure and catalyzes the second through fourth reactions of the fatty acid beta-oxidation cycle. The alpha and beta subunits (HADHA and HADHB) are members of the enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase and 3-ketoacyl-CoA thiolase families, respectively. We analyzed the localization of each of these two genes (HADHA and HADHB) by in situ hybridization and found that both can be assigned to human chromosome band 2p23. Since the distance between the two loci is quite short, the two genes seem to exist side by side, as do the two (A and B subunit) genes of the bacterial fatty acid beta-oxidation multienzyme complex. This is an important and interesting finding in that two entirely different genes, encoding two independent proteins forming a multienzyme complex, are adjacent on chromosome band 2p23.
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收藏
页码:221 / 224
页数:4
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