Recombinant Escherichia coli ATP-dependent Clp protease proteolytic subunit (clpP)

1. Antirestriction activity of the mercury resistance nonconjugative transposon Tn5053 is controlled by the protease ClpXP PMID: 25735133
2. The results demonstrate that ClpXP targets the helicase-nuclease (HsdR) subunit of EcoKI during dsDNA translocation on circular DNA but not on linear DNA. PMID: 25260590
3. Authors found that adoption of a beta-hairpin loop at the N-terminal and the integrity of the hydrophobic cluster at the base of this loop are necessary elements for the axial gate to efficiently translocate protein substrates. PMID: 23927726
4. These results demonstrate that ClpP allosterically impacts the polypeptide translocation activity of ClpA by reducing the cooperativity between ATP binding sites. PMID: 23639359
5. When ClpX encounters a folded protein, it either overcomes this mechanical barrier or slips on the polypeptide before making another unfolding attempt. Binding of ClpP decreases the slip probability and enhances the unfolding efficiency of ClpX. PMID: 21529717
6. data suggest that ClpAP and ClpXP may recognize and bind substrates in significantly different ways PMID: 15591068
7. the main ATP-dependent proteases Lon and ClpP participate in the physiological disintegration of cytoplasmic inclusion bodies, their absence minimizing the protein removal up to 40% PMID: 15967532
8. specific peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP PMID: 16410355
9. the ClpAP-specific adaptor, ClpS, is essential for degradation of N-end rule substrates by ClpAP in bacteria PMID: 16467841
10. ClpXP is a critical factor in the cellular clearance of cytoplasmic RecN aggregates from the cell and therefore plays an important role in DNA damage tolerance PMID: 16914543
11. Discrete static and dynamic interactions mediate binding and communication between ClpX and ClpP. PMID: 17612489
12. ClpS functions, at least in part, as an allosteric effector of ClpAP, broadening understanding of how AAA+ adaptors control substrate selection. PMID: 18297088
13. In the absence of ClpA, deletion of the ClpP N-terminus increases the initial degradation rate of large peptide substrates 5-15-fold. PMID: 18816064
14. Loss of clpP and clpX genes leads to a moderate fourfold increase in spontaneous mutagenesis. PMID: 19040636
15. ClpXP degrades UvrA at different rates during the distinct stages of post-UV recovery when the cells contain different levels of unrepaired cyclobutane pyrimidine dimers. PMID: 19183285
16. analysis of ClpXP adaptors and substrates PMID: 19549779

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KEGG: ecj:JW0427

STRING: 316385.ECDH10B_0393