| Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH. | Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH.
Widjaja MA, Gomez JS, Benson JM, Crowhurst KA., Free PMC Article | 04/17/2021 |
| HdeA binds its substrates heterogeneously, and the "amphiphilic" model for HdeA-substrate interaction is discussed. | Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress.
Yu XC, Yang C, Ding J, Niu X, Hu Y, Jin C. | 11/4/2017 |
| HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA. | HdeB chaperone activity is coupled to its intrinsic dynamic properties.
Ding J, Yang C, Niu X, Hu Y, Jin C., Free PMC Article | 09/24/2016 |
| these results provide insight into the process by which HdeA is primed to unfold and carry out its chaperone duties below pH 3.0 | NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation.
Garrison MA, Crowhurst KA., Free PMC Article | 10/4/2014 |
| During anaerobic growth at pH 5.5, strains deleted for fnr showed enhanced transcription of acid-survival genes gadB, cfa, and hdeA, as well as catalase (katE). | Escherichia coli K-12 survives anaerobic exposure at pH 2 without RpoS, Gad, or hydrogenases, but shows sensitivity to autoclaved broth products.
Riggins DP, Narvaez MJ, Martinez KA, Harden MM, Slonczewski JL., Free PMC Article | 09/14/2013 |
| The small periplasmic chaperone HdeA is directly activated by partial unfolding in a low ph environment. | Chaperone activation by unfolding.
Foit L, George JS, Zhang BW, Brooks CL 3rd, Bardwell JC., Free PMC Article | 06/15/2013 |
| The authors conclude that E. coli O157:H7 strains have evolved acid survival strategies independent of the HdeA/B chaperones and are more acid resistant than nonpathogenic K-12. | Evolutionary silence of the acid chaperone protein HdeB in enterohemorrhagic Escherichia coli O157:H7.
Carter MQ, Louie JW, Fagerquist CK, Sultan O, Miller WG, Mandrell RE., Free PMC Article | 05/5/2012 |
| the partially unfolded character of active HdeA allows the chaperone to adopt different conformations as required for the recognition and high-affinity binding of different substrate proteins. | Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding.
Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC., Free PMC Article | 01/21/2010 |
| Findings show that repression of hdeAB by MarA depends on pH, growth phase, and other regulators of hdeAB and is associated with reduced resistance to acid conditions. | Role of the multidrug resistance regulator MarA in global regulation of the hdeAB acid resistance operon in Escherichia coli.
Ruiz C, McMurry LM, Levy SB., Free PMC Article | 01/21/2010 |
| HdeA and HdeB not only help to maintain proteins in a soluble state during acid treatment, as previously reported, but also assist, both in vitro and in vivo, in the solubilization at neutral pH of mixed protein-chaperone aggregates formed at acidic pH | Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB.
Malki A, Le HT, Milles S, Kern R, Caldas T, Abdallah J, Richarme G. | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | See all PubMed (3) articles | 11/5/2007 |
| HdeA exposes hydrophobic surfaces that appear to be involved in the binding of denatured substrate proteins at extremely low pH values | Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation.
Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B, Chang Z. | 01/21/2010 |