ArticleJournal of molecular biology2012
Salt bridges regulate both dimer formation and monomeric flexibility in HdeB and may have a role in periplasmic chaperone function.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB fromInternational journal of molecular sciences · 2022Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone.The Journal of biological chemistry · 2019Article
- Acid-denatured small heat shock protein HdeA fromThe Journal of biological chemistry · 2019Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Molecular Insights into the Mechanisms of SUN1 Oligomerization in the Nuclear Envelope.Biophysical journal · 2018Article
- Effect of aspartic acid and glutamate on metabolism and acid stress resistance of Acetobacter pasteurianus.Microbial cell factories · 2017Article
- Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistance.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- HdeB chaperone activity is coupled to its intrinsic dynamic properties.Scientific reports · 2015Article
- HdeB functions as an acid-protective chaperone in bacteria.The Journal of biological chemistry · 2015Article
- Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.FEBS open bio · 2015Article
- Chaperone activation by unfolding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Characterization of three novel mechanosensitive channel activities in Escherichia coli.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Escherichia coli and Gram-negative bacteria that live in the human gut must be able to tolerate rapid and large changes in environmental pH. Low pH irreversibly denatures and precipitates many bacterial proteins. While cytoplasmic proteins are well buffered against such swings, periplasmic proteins are not. Instead, it appears that some bacteria utilize chaperone proteins that stabilize periplasmic proteins, preventing their precipitation. Two highly expressed and related proteins, HdeA and HdeB, have been identified as acid-activated chaperones. The structure of HdeA is known and a mechanism for activation has been proposed. In this model, dimeric HdeA dissociates at low pH, and the exposed dimeric interface binds exposed hydrophobic surfaces of acid-denatured proteins, preventing their irreversible aggregation. We now report the structure and biophysical characterization of the HdeB protein. The monomer of HdeB shares a similar structure with HdeA, but its dimeric interface is different in composition and spatial location. We have used fluorescence to study the behavior of HdeB as pH is lowered, and like HdeA, it dissociates to monomers. We have identified one of the key intersubunit interactions that controls pH-induced monomerization. Our analysis identifies a structural interaction within the HdeB monomer that is disrupted as pH is lowered, leading to enhanced structural flexibility.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.