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Single Nucleotide Polymorphism that Accompanies a Missense Mutation (Gln488His) Impedes the Dimerization of Hsp90.


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タイトル: Single Nucleotide Polymorphism that Accompanies a Missense Mutation (Gln488His) Impedes the Dimerization of Hsp90.
著者: Kobayakawa, Takeshi / Yamada, Shin-Ichi / Mizuno, Akio / Ohara-Nemoto, Yuko / Baba, Tomomi T / Nemoto, Takayuki K
発行日: 2009年 1月
出版者: Springer Netherlands
引用: The Protein Journal, 28(1), pp.24-28; 2009
抄録: A single nucleotide polymorphism (SNP) that causes a missense mutation of highly conserved Gln488 to His of the alpha isoform of the 90-kDa heat shock protein (Hsp90alpha) molecular chaperone is observed in Caucasians. The mutated Hsp90alpha severely reduced the growth of yeast cells. To investigate this molecular mechanism, we examined the domain-domain interactions of human Hsp90alpha by using bacterial 2-hybrid system. Hsp90alpha was expressed as a full-length form, N-terminal domain (residues 1-400), or middle (residues 401-617) plus C-terminal (residues 618-732) domains (MC domain/amino acids 401-732). The Gln488His substitution in MC domain did not affect the intra-molecular interaction with N-terminal domain, whereas the dimeric interaction-mediated by the inter-molecular interaction between MC domains was decreased to 32%. Gln488Ala caused a similar change, whereas Gln488Thr, which exceptionally occurs in mitochondrial Hsp90 paralog, fully maintained the dimeric interaction. Therefore, the SNP causing Gln488His mutation could abrogate the Hsp90 function due to reduced dimerization.
キーワード: Dimer formation / Hsp90 / Missense mutation / SNP / Trap1
URI: http://hdl.handle.net/10069/20950
ISSN: 15723887
DOI: 10.1007/s10930-008-9160-1
PubMed ID: 19130193
権利: (c) Springer Science+Business Media, LLC 2008 / The original publication is available at www.springerlink.com
資料タイプ: Journal Article
原稿種類: author
出現コレクション:040 学術雑誌論文

引用URI : http://hdl.handle.net/10069/20950

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