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A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone.
http://hdl.handle.net/10069/20092
http://hdl.handle.net/10069/20092deb9c568-3975-47a3-a05d-fed8f87dcd1f
名前 / ファイル | ライセンス | アクション |
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EJB27_1_146.pdf (412.5 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2008-10-16 | |||||
タイトル | ||||||
タイトル | A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone. | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | GRP94 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | HtpG | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | molecular chaperone | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | dimer | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | client binding | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Yamada, Shin-ichi
× Yamada, Shin-ichi× Ono, Toshio× Mizuno, Akio× Nemoto, Takayuki K |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The alpha isoform of human 90-kDa heat shock protein (HSP90alpha) is composed of three domains: the N-terminal (residues 1-400); middle (residues 401-615) and C-terminal (residues 621-732). The middle domain is simultaneously associated with the N- and C-terminal domains, and the interaction with the latter mediates the dimeric configuration of HSP90. Besides one in the N-terminal domain, an additional client-binding site exists in the C-terminal domain of HSP90. The aim of the present study is to elucidate the regions within the C-terminal domain responsible for the bindings to the middle domain and to a client protein, and to define the relationship between the two functions. A bacterial two-hybrid system revealed that residues 650-697 of HSP90alpha were essential for the binding to the middle domain. An almost identical region (residues 657-720) was required for the suppression of heat-induced aggregation of citrate synthase, a model client protein. Replacement of either Leu665-Leu666 or Leu671-Leu672 to Ser-Ser within the hydrophobic segment (residues 662-678) of the C-terminal domain caused the loss of bindings to both the middle domain and the client protein. The interaction between the middle and C-terminal domains was also found in human 94-kDa glucose-regulated protein. Moreover, Escherichia coli HtpG, a bacterial HSP90 homologue, formed heterodimeric complexes with HSP90alpha and the 94-kDa glucose-regulated protein through their middle-C-terminal domains. Taken together, it is concluded that the identical region including the hydrophobic segment of the C-terminal domain is essential for both the client binding and dimer formation of the HSP90-family molecular chaperone and that the dimeric configuration appears to be similar in the HSP90-family proteins. | |||||
書誌情報 |
European journal of biochemistry / FEBS 巻 270, 号 1, p. 146-154, 発行日 2003-01 |
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出版者 | ||||||
出版者 | Blackwell Science | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 00142956 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00639541 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 12492485 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1046/j.1432-1033.2003.03375.x | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | European journal of biochemistry, 270(1), pp.146-154; 2003 |