Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction

HSP-100 protein machines, such as ClpB, play an essential role in reactivating protein aggregates that can otherwise be lethal to cells. Although the players involved are known, including the DnaK/DnaJ/GrpE chaperone system in bacteria, details of the molecular interactions are not well understood....

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2013-03, Vol.339 (6123), p.1080-1083
Hauptverfasser:	Rosenzweig, Rina, Moradi, Shoeib, Zarrine-Afsar, Arash, Glover, John R., Kay, Lewis E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphatases Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Aggregates Bacteria Bacterial Proteins - chemistry Binding sites Biochemistry Cell aggregates Channels Genetic mutation Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Hydrolysis Meningioma Models, Chemical Molecular structure Mutation Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Nucleotides Polypeptides Protein folding Protein Interaction Domains and Motifs Protein Interaction Maps Protein Multimerization Protein Refolding Protein Structure, Tertiary Protein Transport Proteins Quality Control Solubilization Thermus thermophilus Titration
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