@article{oai:nagasaki-u.repo.nii.ac.jp:00016298,
 author = {Matsumoto, Shigeki and Tanaka, Etsuko and Nemoto, Takayuki K and Ono, Toshio and Takagi, Takashi and Imai, Jun and Kimura, Yoko and Yahara, Ichiro and Kobayakawa, Takeshi and Ayuse, Takao and Oi, Kumiko and Mizuno, Akio},
 issue = {38},
 journal = {The Journal of biological chemistry},
 month = {Sep},
 note = {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., Journal of Biological Chemistry, Vol. 277, Issue 38, 34959-34966, September 20, 2002},
 pages = {34959--34966},
 title = {Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.},
 volume = {277},
 year = {2002}
}