scholarly journals Aggregate reactivation mediated by the Hsp100 chaperones

2012 ◽  
Vol 520 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Michal Zolkiewski ◽  
Ting Zhang ◽  
Maria Nagy
Keyword(s):  
Hsp100 Chaperones

scholarly journals Successive and Synergistic Action of the Hsp70 and Hsp100 Chaperones in Protein Disaggregation

2004 ◽  
Vol 279 (43) ◽  
pp. 44376-44383 ◽  
Author(s):  
Szymon Ziȩtkiewicz ◽  
Joanna Krzewska ◽  
Krzysztof Liberek
Keyword(s):  
Synergistic Action ◽  
Hsp100 Chaperones

scholarly journals Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation

2012 ◽  
Vol 198 (3) ◽  
pp. 387-404 ◽  
Author(s):  
Juliane Winkler ◽  
Jens Tyedmers ◽  
Bernd Bukau ◽  
Axel Mogk
Keyword(s):  
Protein Aggregates ◽  
Specific Targeting ◽  
Terminal Domain ◽  
Independent Association ◽  
Species Specific ◽  
Almost All ◽  
Hsp100 Chaperones

Hsp100 and Hsp70 chaperones in bacteria, yeast, and plants cooperate to reactivate aggregated proteins. Disaggregation relies on Hsp70 function and on ATP-dependent threading of aggregated polypeptides through the pore of the Hsp100 AAA+ hexamer. In yeast, both chaperones also promote propagation of prions by fibril fragmentation, but their functional interplay is controversial. Here, we demonstrate that Hsp70 chaperones were essential for species-specific targeting of their Hsp100 partner chaperones ClpB and Hsp104, respectively, to heat-induced protein aggregates in vivo. Hsp70 inactivation in yeast also abrogated Hsp104 targeting to almost all prions tested and reduced fibril mobility, which indicates that fibril fragmentation by Hsp104 requires Hsp70. The Sup35 prion was unique in allowing Hsp70-independent association of Hsp104 via its N-terminal domain, which, however, was nonproductive. Hsp104 overproduction even outcompeted Hsp70 for Sup35 prion binding, which explains why this condition prevented Sup35 fragmentation and caused prion curing. Our findings indicate a conserved mechanism of Hsp70–Hsp100 cooperation at the surface of protein aggregates and prion fibrils.

Crowbars and ratchets: Hsp100 chaperones as tools in reversing protein aggregation

2001 ◽  
Vol 79 (5) ◽  
pp. 557-568 ◽  
Author(s):  
John R Glover ◽  
John M Tkach
Keyword(s):  
Protein Synthesis ◽  
Protein Aggregation ◽  
Molecular Chaperone ◽  
Molecular Chaperones ◽  
Recent Progress ◽  
Chemical Stress ◽  
Intracellular Aggregates ◽  
Physical And Chemical ◽  
Hsp100 Chaperones

Molecular chaperones have the capacity to prevent inappropriate interactions between aggregation-prone folding or unfolding intermediates created in the cell during protein synthesis or in response to physical and chemical stress. What happens when surveillance by molecular chaperones is evaded or overwhelmed and aggregates accumulate? Recent progress in the elucidation of Hsp100/Clp function suggests that intracellular aggregates or stable complexes can be progressively dissolved by the action of chaperones that act as molecular crowbars or ratchets. These insights set the stage for new progress in the understanding and treatment of diseases of protein folding.Key words: molecular chaperone, Hsp100, aggregation, amyloid.

scholarly journals Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities

2011 ◽  
Vol 17 (3) ◽  
pp. 361-373 ◽  
Author(s):  
Łukasz Nowicki ◽  
Paweł Leźnicki ◽  
Ewa Morawiec ◽  
Natalia Litwińczuk ◽  
Krzysztof Liberek
Keyword(s):  
Aspartic Acid ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Nucleotide Binding Domain 1 ◽  
Hsp100 Chaperones

scholarly journals Protein Binding and Disruption by Clp/Hsp100 Chaperones

Structure ◽  
2004 ◽  
Vol 12 (2) ◽  
pp. 175-183 ◽  
Author(s):  
Michael R. Maurizi ◽  
Di Xia
Keyword(s):  
Protein Binding ◽  
Hsp100 Chaperones

scholarly journals Toward a unified model of the action of CLP/HSP100 chaperones in chloroplasts

2012 ◽  
Vol 7 (6) ◽  
pp. 672-674 ◽  
Author(s):  
Germán L. Rosano ◽  
Eduardo M. Bruch ◽  
Clara V. Colombo ◽  
Eduardo A. Ceccarelli
Keyword(s):  
Unified Model ◽  
Hsp100 Chaperones

scholarly journals Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis

PLoS Genetics ◽  
2016 ◽  
Vol 12 (1) ◽  
pp. e1005824 ◽  
Author(s):  
Pablo Pulido ◽  
Ernesto Llamas ◽  
Briardo Llorente ◽  
Salvador Ventura ◽  
Louwrance P. Wright ◽  
...  
Keyword(s):  
Clp Protease ◽  
Isoprenoid Pathway ◽  
Hsp100 Chaperones
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