Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain

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• 作者：Masaki Takahashi ; Mineyuki Mizuguchi ; Hiroyuki Shinoda ; Tomoyasu Aizawa ; Makoto Demura ; Hitoshi Okazawa ; Keiichi Kawano
• 关键词：Unstructured protein ; Protein structure ; PQBP-1 ; Polyglutamine ; U5-15kD
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2010
• 出版时间：July 2010
• 年：2010
• 卷：1804
• 期：7
• 页码：1500-1507
• 全文大小：985 K

文摘

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.