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Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.
http://hdl.handle.net/10069/22177
http://hdl.handle.net/10069/221772db56d31-152f-4ee4-88c5-532a77c3b3a9
名前 / ファイル | ライセンス | アクション |
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JBC_277_38_34959.pdf (479.7 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2009-09-17 | |||||
タイトル | ||||||
タイトル | Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone. | |||||
言語 | ||||||
言語 | eng | |||||
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 |
Matsumoto, Shigeki
× Matsumoto, Shigeki× Tanaka, Etsuko× Nemoto, Takayuki K× Ono, Toshio× Takagi, Takashi× Imai, Jun× Kimura, Yoko× Yahara, Ichiro× Kobayakawa, Takeshi× Ayuse, Takao× Oi, Kumiko× Mizuno, Akio |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | At the primary structure level, the 90-kDa heat shock protein (HSP90) is composed of three regions: the N-terminal (Met(1)-Arg(400)), middle (Glu(401)-Lys(615)), and C-terminal (Asp(621)-Asp(732)) regions. In the present study, we investigated potential subregion structures of these three regions and their roles. Limited proteolysis revealed that the N-terminal region could be split into two fragments carrying residues Met(1) to Lys(281) (or Lys(283)) and Glu(282) (or Tyr(284)) to Arg(400). The former is known to carry the ATP-binding domain. The fragments carrying the N-terminal two-thirds (Glu(401)-Lys(546)) and C-terminal one-third of the middle region were sufficient for the interactions with the N- and C-terminal regions, respectively. Yeast HSC82 that carried point mutations in the middle region causing deficient binding to the N-terminal region could not support the growth of HSP82-depleted cells at an elevated temperature. Taken together, our data show that the N-terminal and middle regions of the HSP90 family protein are structurally divided into two respective subregions. Moreover, the interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 in yeast. | |||||
書誌情報 |
The Journal of biological chemistry 巻 277, 号 38, p. 34959-34966, 発行日 2002-09-20 |
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出版者 | ||||||
出版者 | American Society for Biochemistry and Molecular Biology | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 00219258 | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1083-351X | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00251083 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 12121981 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1074/jbc.M203038200 | |||||
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 | Journal of Biological Chemistry, Vol. 277, Issue 38, 34959-34966, September 20, 2002 |