Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain |
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| Authors: | Masaki Takahashi Mineyuki Mizuguchi Hiroyuki Shinoda Tomoyasu Aizawa Makoto Demura Hitoshi Okazawa Keiichi Kawano |
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| Affiliation: | 1. Faculty of Pharmaceutical Sciences, University of Toyama, 2630, Sugitani, Toyama 930-0194, Japan;2. Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan;3. Department of Neuropathology, Medical Research Institute, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo 113-8510, Japan |
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| Abstract: | Polyglutamine tract-binding protein-1 (PQBP-1) is a nuclear protein that interacts with various proteins, including RNA polymerase II and the spliceosomal protein U5-15kD. PQBP-1 is known to be associated with X-linked mental retardation in which a frameshift mutation in the PQBP-1 gene occurs. In the present study, we demonstrate that PQBP-1 binds to U5-15kD via a continuous 23-residue segment within its C-terminal domain. Intriguingly, this segment is lost in the frameshift mutants of PQBP-1 associated with X-linked mental retardation. These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD. |
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| Keywords: | hDim2, human Dim2 HSQC, heteronuclear single-quantum correlation PQBP-1, polyglutamine tract-binding protein-1 PQBP-1-CT43, PQBP-1(223&ndash 265) snRNP, small nuclear ribonucleoprotein particle XLMR, X-linked mental retardation |
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