Abstract
Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. The poly-Q tracts show extensive variation in both the number and the configuration of repeats among species. A surface plasmon resonance assay showed clear interaction between human PQBP-1 and Q11, representative of the poly-Q tract of the ataxin-1 of Old World monkeys. No response was observed using Q2PQ2P4Q2, representative of the poly-Q tract of the ataxin-1 of New World monkeys. This implies that the interaction of human PQBP-1 with ataxin-1 is limited to humans and closely related species. Comparison of the human and mouse PQBP-1 sequences showed an elevated amino acid substitution rate in the polar amino acid-rich domain of PQBP-1 that is responsible for binding to poly-Q tracts. This could have been advantageous to the new biological function of human PQBP-1 through poly-Q tracts.
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This study was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan.
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Kurosaki, T., Gojobori, J. & Ueda, S. Comparative Genetics of the Poly-Q Tract of Ataxin-1 and Its Binding Protein PQBP-1. Biochem Genet 50, 309–317 (2012). https://doi.org/10.1007/s10528-011-9473-1
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DOI: https://doi.org/10.1007/s10528-011-9473-1