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


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Title: Single Nucleotide Polymorphism that Accompanies a Missense Mutation (Gln488His) Impedes the Dimerization of Hsp90.
Authors: Kobayakawa, Takeshi / Yamada, Shin-Ichi / Mizuno, Akio / Ohara-Nemoto, Yuko / Baba, Tomomi T / Nemoto, Takayuki K
Issue Date: Jan-2009
Publisher: Springer Netherlands
Citation: The Protein Journal, 28(1), pp.24-28; 2009
Abstract: 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.
Keywords: 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
Rights: (c) Springer Science+Business Media, LLC 2008 / The original publication is available at www.springerlink.com
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

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

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