| ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. | Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.
Deville C, Franke K, Mogk A, Bukau B, Saibil HR., Free PMC Article | 07/18/2020 |
| Suggest possible role of E. coli ClpB in the molecular signaling cascade of protein-induced satiety. | Effects of Macronutrients on the In Vitro Production of ClpB, a Bacterial Mimetic Protein of α-MSH and Its Possible Role in Satiety Signaling.
Dominique M, Breton J, Guérin C, Bole-Feysot C, Lambert G, Déchelotte P, Fetissov S., Free PMC Article | 02/29/2020 |
| The authors find that large aggregates or bulky, native-like substrates activate the DnaK-ClpB complex, whereas a smaller, permanently unfolded protein or extended, short peptides fail to stimulate it. | Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.
Fernández-Higuero JA, Aguado A, Perales-Calvo J, Moro F, Muga A., Free PMC Article | 10/12/2019 |
| The authors show here that both Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 cooperation with their cognate Hsp70 is crucial for efficient protein disaggregation and, in contrast to earlier claims, cannot be circumvented by activating M-domain mutations. | Bacterial and Yeast AAA+ Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70.
Kummer E, Szlachcic A, Franke KB, Ungelenk S, Bukau B, Mogk A. | 06/24/2017 |
| This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. | Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.
Zolkiewski M, Chesnokova LS, Witt SN., Free PMC Article | 10/29/2016 |
| Studied the dynamic assembly equilibrium for E. coli ClpB | Examination of the dynamic assembly equilibrium for E. coli ClpB.
Lin J, Lucius AL. | 07/30/2016 |
| Data show that E coli can propagate the Sup35 prion, which requires disaggregase activity of the heat shock protein ClpB chaperone. | Prion propagation can occur in a prokaryote and requires the ClpB chaperone.
Yuan AH, Garrity SJ, Nako E, Hochschild A., Free PMC Article | 06/27/2015 |
| ClpB hexamers remain associated during several ATP hydrolysis events required to translocate substrates through the protein central channel. | ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins.
Aguado A, Fernández-Higuero JA, Cabrera Y, Moro F, Muga A. | 05/2/2015 |
| E. coli DnaK variants with substitutions in subdomains IB and IIB of the nucleotide-binding domain are defective for in vivo and in vitro interactions with ClpB. | Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.
Doyle SM, Shastry S, Kravats AN, Shih YH, Miot M, Hoskins JR, Stan G, Wickner S., Free PMC Article | 03/21/2015 |
| Data indicate that ClpB requires DnaK more stringently than Hsp104 requires Hsp70 for protein disaggregation. | Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.
Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J., Free PMC Article | 04/12/2014 |
| Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB | [Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB].
Mel'kina OE, Gorianin II, Manukhov IV, Zavil'gel'skiĭ GB. | 08/31/2013 |
| Produced 7 variants of ClpB w/modified sequence of the N-terminal linker to study conformational flexibility. We conclude the linker does not merely connect the N-terminal domain, but contributes to efficiency of aggregate binding and disaggregation. | Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.
Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, Smith PE, Zolkiewski M., Free PMC Article | 06/15/2013 |
| Mutations intended to disrupt the putative ionic interactions in yeast Hsp104 and bacterial ClpB disaggregases resulted in remarkable changes of their biochemical properties | Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.
Lipińska N, Ziętkiewicz S, Sobczak A, Jurczyk A, Potocki W, Morawiec E, Wawrzycka A, Gumowski K, Ślusarz M, Rodziewicz-Motowidło S, Chruściel E, Liberek K., Free PMC Article | 04/6/2013 |
| The wt hexamer can accommodate two mutant sub units that hydrolyze ATP in only one protein ring. Four subunits seem to build the functional cooperative unit, provided that one of the protein rings contains active nucleotide binding sites. | Nucleotide utilization requirements that render ClpB active as a chaperone.
del Castillo U, Fernández-Higuero JA, Pérez-Acebrón S, Moro F, Muga A. | 03/22/2010 |
| The authors found that ClpB95 and ClpB80 form hetero-oligomers, which are similar in size to the homo-oligomers of ClpB95 or ClpB80. | Synergistic cooperation between two ClpB isoforms in aggregate reactivation.
Nagy M, Guenther I, Akoyev V, Barnett ME, Zavodszky MI, Kedzierska-Mieszkowska S, Zolkiewski M., Free PMC Article | 03/15/2010 |
| mechanism by which ClpB couples ATP utilization to protein remodeling with and without the DnaK system | Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein.
Hoskins JR, Doyle SM, Wickner S., Free PMC Article | 02/22/2010 |
| N-terminus verified by Edman degradation on complete protein | ClpB proteins copurify with the anaerobic Escherichia coli reductase.
Pontis E, Sun XY, Jörnvall H, Krook M, Reichard P. | 11/5/2007 |
| Certain conformational properties (in particular, beta-structures) of subunits forming these aggregates are the most important factor determining the necessity of the ClpB chaperone in the disaggregation process. | Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process.
Lewandowska A, Matuszewska M, Liberek K. | 01/21/2010 |
| ClpB and the DnaK system act synergistically to remodel proteins and dissolve aggregates. | Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system.
Doyle SM, Hoskins JR, Wickner S., Free PMC Article | 01/21/2010 |
| E. coli maintains the ClpB80 to ClpB95 isoforms ratio at a nearly constant value of 0.4-0.5 under a variety of stress conditions. | Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress.
Chow IT, Baneyx F. | 01/21/2010 |
| the N-terminal domain of ClpB has an essential role in recognizing and binding strongly aggregated proteins | The amino-terminal domain of ClpB supports binding to strongly aggregated proteins.
Barnett ME, Nagy M, Kedzierska S, Zolkiewski M. | 01/21/2010 |
| N-terminus of ClpB95 isoform interferes with its in vivo and in vitro activity | The N-terminal domain of Escherichia coli ClpB enhances chaperone function.
Chow IT, Barnett ME, Zolkiewski M, Baneyx F. | 01/21/2010 |
| These results revealed that conserved amino acids Thr7 and Ser84 both participated in maintaining the conformational integrity of the ClpB N-terminal domain. | The roles of conserved amino acids on substrate binding and conformational integrity of ClpB N-terminal domain.
Tanaka N, Tani Y, Tada T, Lee YF, Kanaori K, Kunugi S. | 01/21/2010 |
| the conserved helix 3 of the M domain is specifically required for the DnaK-dependent shuffling of aggregated proteins, but not of soluble denatured substrates, to the pore entrance of the ClpB translocation channel. | M domains couple the ClpB threading motor with the DnaK chaperone activity.
Haslberger T, Weibezahn J, Zahn R, Lee S, Tsai FT, Bukau B, Mogk A. | 01/21/2010 |
| in the chaperone-dependent disaggregation process, DnaK and DnaJ bind to aggregates prior to ClpB action | Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation.
Zietkiewicz S, Krzewska J, Liberek K. | 01/21/2010 |