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Substitution of only two residues of human Hsp90alpha causes impeded dimerization of Hsp90beta.


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Title: Substitution of only two residues of human Hsp90alpha causes impeded dimerization of Hsp90beta.
Authors: Kobayakawa, Takeshi / Yamada, Shin-Ichi / Mizuno, Akio / Nemoto, Takayuki K
Issue Date: Mar-2008
Publisher: Springer Netherlands
Citation: Cell Stress and Chaperones, 13(1), pp.97-104; 2008
Abstract: Two isoforms of the 90-kDa heat-shock protein (Hsp90), i.e., Hsp90alpha and Hsp90beta, are expressed in the cytosol of mammalian cells. Although Hsp90 predominantly exists as a dimer, the dimer-forming potential of the beta isoform of human and mouse Hsp90 is less than that of the alpha isoform. The 16 amino acid substitutions located in the 561-685 amino acid region of the C-terminal dimerization domain should be responsible for this impeded dimerization of Hsp90beta (Nemoto T, Ohara-Nemoto Y, Ota M, Takagi T, Yokoyama K. Eur J Biochem 233: 1-8, 1995). The present study was performed to define the amino acid substitutions that cause the impeded dimerization of Hsp90beta. Bacterial two-hybrid analysis revealed that among the 16 amino acids, the conversion from Ala(558) of Hsp90beta to Thr(566) of Hsp90alpha and that from Met(621) of Hsp90beta to Ala(629) of Hsp90alpha most efficiently reversed the dimeric interaction, and that the inverse changes from those of Hsp90alpha to Hsp90beta primarily explained the impeded dimerization of Hsp90beta We conclude that taken together, the conversion of Thr(566) and Ala(629) of Hsp90alpha to Ala(558) and Met(621) is primarily responsible for impeded dimerization of Hsp90beta.
Keywords: Hsp90 / Dimerization / Amino acid substitution / Molecular chaperone
URI: http://hdl.handle.net/10069/20059
ISSN: 13558145
DOI: 10.1007/s12192-008-0017-5
PubMed ID: 18347946
Rights: © Cell Stress Society International 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/10069/20059

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