| Autor: |
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 |
| Zdroj: |
Journal of Biological Chemistry; September 2002, Vol. 277 Issue: 38 p34959-66, 8p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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