DSpace university logo mark
Advanced Search
Japanese | English 

NAOSITE : Nagasaki University's Academic Output SITE > School of Dentistry > Articles in academic journal >

Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.


File Description SizeFormat
JBC_277_38_34959.pdf468.45 kBAdobe PDFView/Open

Title: Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.
Authors: 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
Issue Date: 20-Sep-2002
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry, Vol. 277, Issue 38, 34959-34966, September 20, 2002
Abstract: 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.
URI: http://hdl.handle.net/10069/22177
ISSN: 00219258
DOI: 10.1074/jbc.M203038200
PubMed ID: 12121981
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/22177

All items in NAOSITE are protected by copyright, with all rights reserved.

 

Valid XHTML 1.0! Copyright © 2006-2015 Nagasaki University Library - Feedback Powerd by DSpace