Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

Shinji Tsutsumi, Mehdi Mollapour, Chrisostomos Prodromou, Chung-Tien Lee, Barry Panaretou, Soichiro Yoshida, Matthias P. Mayer and Leonard M. Neckers
Proceedings of the National Academy of Sciences of the United States of America
Vol. 109, No. 8 (February 21, 2012), pp. 2937-2942
Stable URL: http://www.jstor.org/stable/41506871
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity
Preview not available

Abstract

Hsp90 is an essential and highly conserved modular molecular chaperone whose N and middle domains are separated by a disordered region termed the charged linker. Although its importance has been previously disregarded, because a minimal linker length is sufficient for Hsp90 activity, the evolutionary persistence of extensive charged linkers of divergent sequence in Hsp90 proteins of most eukaryotes remains unexplained. To examine this question further, we introduced human and plasmodium native and length-matched artificial linkers into yeast Hsp90. After evaluating ATPase activity and biophysical characteristics in vitro, and chaperone function in vivo, we conclude that linker sequence affects Hsp90 function, cochaperone interaction, and conformation. We propose that the charged linker, in addition to providing the flexibility necessary for Hsp90 domain rearrangements—likely its original purpose—has evolved in eukaryotes to serve as a rheostat for the Hsp90 chaperone machine.

Page Thumbnails

  • Thumbnail: Page 
[2937]
    [2937]
  • Thumbnail: Page 
2938
    2938
  • Thumbnail: Page 
2939
    2939
  • Thumbnail: Page 
2940
    2940
  • Thumbnail: Page 
2941
    2941
  • Thumbnail: Page 
2942
    2942