PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain.
PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain.
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DOI：
10.1006/bbrc.2000.2992
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发表时间：
2000-07
影响因子：
3.1
通讯作者：
Masaaki Waragai;E. Junn;M. Kajikawa;S. Takeuchi;Ichiro Kanazawa;M. Shibata;M. Mouradian;Hitoshi Okazawa
中科院分区：
文献类型：
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作者：
Masaaki Waragai;E. Junn;M. Kajikawa;S. Takeuchi;Ichiro Kanazawa;M. Shibata;M. Mouradian;Hitoshi Okazawa
PQBP-1被鉴定为存在于各种转录相关因子和神经退行性疾病的致病基因中的多聚谷氨酰胺束的结合蛋白。该基因至少包含两个功能结构域，WW结构域和羧基末端结构域（CTD）。虽然人PQBP-1还含有极性氨基酸丰富的结构域，它通过该结构域与多聚谷氨酰胺束结合，但真正的生理功能尚未阐明。在本研究中，我们发现，U 5 - 15 kD，裂殖酵母dim 1 p的人类同源物，是PQBP-1与CTD结合的伴侣分子。这一发现表明PQBP-1在剪接、细胞周期和泛素化中的生理功能，从而推测PQBP-1在三联体重复疾病中的病理作用。
PQBP-1 was identified as a binding protein to the polyglutamine tract present in various transcription-related factors and causative genes for neurodegenerative disorders. This novel gene contains at least two functional domains, WW domain and carboxyl-terminal domain (CTD), strictly conserved beyond species. Although human PQBP-1 additionally contains the polar amino acid-rich domain by which it binds to the polyglutamine tract, genuine physiological function(s) have not been clarified. In this study, we showed that U5-15kD, human homologue of fission yeast dim1p, is a partner molecule of PQBP-1 binding to CTD. This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases.