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.
雑誌名
The Journal of biological chemistry
巻
277
号
38
ページ
34959 - 34966
発行年
2002-09-20
出版者
American Society for Biochemistry and Molecular Biology
ISSN
00219258
EISSN
1083-351X
書誌レコードID
AA00251083
PubMed番号
12121981
DOI
10.1074/jbc.M203038200
著者版フラグ
author
引用
Journal of Biological Chemistry, Vol. 277, Issue 38, 34959-34966, September 20, 2002
Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.
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