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Article

The amino-terminal domain of ClpB supports binding to strongly aggregated proteins.

The Journal of biological chemistry - 14 Oct 2005

Barnett Micheal E, Nagy Maria, Kedzierska Sabina, Zolkiewski Michal

Abstract excerpt

Bacterial heat-shock proteins, ClpB and DnaK form a bichaperone system that efficiently reactivates aggregated proteins. ClpB undergoes nucleotide-dependent self-association and forms ring-shaped oligomers. The ClpB-assisted dissociation of protein aggregates is linked to translocation of substrates through the central channel in the oligomeric ClpB. Events preceding the translocation step, such as recognition of...

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PMID: 16076845
DOI: 10.1074/jbc.M505653200

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The amino-terminal domain of ClpB supports binding to strongly aggregated proteins.PMID 16076845Read ↗

Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity.Semantic proximity Read ↗

Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.Semantic proximity Read ↗

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Semantic proximity Read ↗

Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Semantic proximity Read ↗

Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein.Semantic proximity Read ↗

Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.Semantic proximity Read ↗

Characterization of a trap mutant of the AAA+ chaperone ClpB.Semantic proximity Read ↗

Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli.Semantic proximity Read ↗

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.Semantic proximity Read ↗

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.Semantic proximity Read ↗

ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2.Semantic proximity Read ↗

C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding.Semantic proximity Read ↗

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