Recombinant Escherichia coli Chaperone protein ClpB (clpB), partial

1. 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. PMID: 27616763
2. Studied the dynamic assembly equilibrium for E. coli ClpB PMID: 26313457
3. Data show that E coli can propagate the Sup35 prion, which requires disaggregase activity of the heat shock protein ClpB chaperone. PMID: 25122461
4. ClpB hexamers remain associated during several ATP hydrolysis events required to translocate substrates through the protein central channel. PMID: 25558912
5. 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. PMID: 22890624
6. Mutations intended to disrupt the putative ionic interactions in yeast Hsp104 and bacterial ClpB disaggregases resulted in remarkable changes of their biochemical properties PMID: 23233670
7. 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. PMID: 20085762
8. The authors found that ClpB95 and ClpB80 form hetero-oligomers, which are similar in size to the homo-oligomers of ClpB95 or ClpB80. PMID: 19961856
9. mechanism by which ClpB couples ATP utilization to protein remodeling with and without the DnaK system PMID: 19940245
10. 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. PMID: 16038902
11. N-terminus of ClpB95 isoform interferes with its in vivo and in vitro activity PMID: 16051221
12. the N-terminal domain of ClpB has an essential role in recognizing and binding strongly aggregated proteins PMID: 16076845
13. These results revealed that conserved amino acids Thr7 and Ser84 both participated in maintaining the conformational integrity of the ClpB N-terminal domain. PMID: 16834329
14. 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. PMID: 17244532
15. 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. PMID: 17588600

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KEGG: ecj:JW2573

STRING: 316385.ECDH10B_2760