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Science Forum Index » Life Extension Forum » Redox regulated chaperone network
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| Tim |
 Posted: Fri Jan 02, 2004 10:37 am |
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EMBO J. 2003 Dec 11 [Epub ahead of print]. Related Articles, Links
Identification of a redox-regulated chaperone network.
Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U.
Department of Molecular, Cellular and Developmental Biology,
University of Michigan, Ann Arbor, MI, USA.
We have identified and reconstituted a multicomponent redox-chaperone
network that appears to be designed to protect proteins against
stress-induced unfolding and to refold proteins when conditions return
to normal. The central player is Hsp33, a redox-regulated molecular
chaperone. Hsp33, which is activated by disulfide bond formation and
subsequent dimerization, works as an efficient chaperone holdase that
binds to unfolding protein intermediates and maintains them in a
folding competent conformation. Reduction of Hsp33 is catalyzed by the
glutaredoxin and thioredoxin systems in vivo, and leads to the
formation of highly active, reduced Hsp33 dimers. Reduction of Hsp33
is necessary but not sufficient for substrate protein release.
Substrate dissociation from Hsp33 is linked to the presence of the
DnaK/DnaJ/GrpE foldase system, which alone, or in concert with the
GroEL/GroES system, then supports the refolding of the substrate
proteins. Upon substrate release, reduced Hsp33 dimers dissociate into
inactive monomers. This regulated substrate transfer ultimately links
substrate release and Hsp33 inactivation to the presence of available
DnaK/DnaJ/GrpE, and, therefore, to the return of cells to non-stress
conditions.
PMID: 14685279 [PubMed - as supplied by publisher] |
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| Tim Tyler |
| Posted: Fri Jan 02, 2004 11:19 am |
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Tim <timothytn@my-deja.com> wrote or quoted:
[...]
Quote: Identification of a redox-regulated chaperone network. [...]
We have identified and reconstituted a multicomponent redox-chaperone
network that appears to be designed to protect proteins against
stress-induced unfolding and to refold proteins when conditions
return to normal. [...]
PMID: 14685279 [PubMed - as supplied by publisher]
Significant theraputic potential there - by the sound of it 
--
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|im |yler http://timtyler.org/ tim@tt1lock.org Remove lock to reply. |
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