degP Antibody

1. Our results suggest that YjfN is a novel "suicide activator" for DegP that enhances DegP proteolysis under misfolded protein stress. PMID: 28947671
2. Investigated the influence of amino acid substitutions located within the LD loop on the kinetics of a model substrate cleavage as well as on the dynamics of the oligomeric structure of HtrA. We found that the mutations that were expected to disturb the loop's structure and/or interactions with the remaining regulatory loops severely diminished the proteolytic activity of HtrA. PMID: 27469236
3. In the present review, we summarize recent advances in the characterization of these key factors, with a special emphasis on the multifunctional protein DegP. PMID: 25849907
4. The lack of the disulfide within LA affected the stability and the overall structure of the HtrA molecule. PMID: 25710793
5. Sensitive activation and cage assembly needs covalent linkage of distinct substrate sequences that affect degradation (degrons); 1 degron binds the DegP active site, a 2nd degron binds a separate tethering site in PDZ1 of a substrate-bound DegP dodecamer. PMID: 21458668
6. Formation of contacts between the apical parts (residues 231-234) of the L2 loops within the HtrA trimer, in particular the residue D232, was shown to play a crucial role in the activation process of HtrA. PMID: 20515644
7. Effector-peptide binding to the PDZ domain of DegP induces oligomer conversion from resting hexameric DegP6 into proteolytically active 12-mers and 24-mers. PMID: 20581825
8. The combined introduction of loop L2 and PDZ domain 1 of DegP into DegS converted DegS even further into a DegP-like protease. PMID: 20184896
9. the osmoregulation of the expression of htrA gene; role of the nucleoid associated proteins H-NS and Hha in the repression of htrA expression at low osmolarity PMID: 16143461
10. the N-terminal alpha-helix is an important functional domain for inhibition of the Cpx pathway and that CpxP is subject to DegP-dependent proteolysis PMID: 16166523
11. CpxP functions as a periplasmic adaptor protein that is required for the effective proteolysis of a subset of misfolded substrates by the DegP protease PMID: 16303867
12. Results show that the functional unit for the protease and chaperone activities of DegP is a trimer and that neither a cavity of specific dimensions nor the presence of an enclosed cavity appears to be essential for its protease and chaperone activities. PMID: 17122339
13. HtrA may protect the bacterial cells from deleterious effects of heat shock not only by degrading the damaged proteins but by combination of the proteolytic and chaperoning activities PMID: 17485069
14. This article summarizes recent studies regarding the HtrA family of proteins, their structure, regulation and function. It also presents practical applications of this knowledge and perspective of its use in the future. PMID: 17718385
15. HtrA can in fact act as a protease at low temperatures. PMID: 19047732
16. Review show that DegP adopts various forms, depending on the surrounding environment and the availability of a substrate. PMID: 19465652

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KEGG: ecj:JW0157

STRING: 316385.ECDH10B_0141