ArticleProceedings of the National Academy of Sciences of the United States of America2016
Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Quantitative transcriptomic and metabolic analyses reveal the roles of RpoS and Crp in the acid resistance system 1 inMicrobiology spectrum · 2026Article
- STK-mediated FadR phosphorylation regulates the acid resistance and virulence of Streptococcus suis.PLoS pathogens · 2025Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB fromInternational journal of molecular sciences · 2022Article
- mRNA-Seq reveals the quorum sensing system luxS gene contributes to the environmental fitness of Streptococcus suis type 2.BMC microbiology · 2021Article
- Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH.Biochimica et biophysica acta. Proteins and proteomics · 2021Article
- Halo-fluorescein for photodynamic bacteria inactivation in extremely acidic conditions.Nature communications · 2021Article
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- 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
- Compartmentalizing acid stress in bacteria.Nature chemical biology · 2018Article
- In vivo chloride concentrations surge to proteotoxic levels during acid stress.Nature chemical biology · 2018Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- The Mechanism of HdeA Unfolding and Chaperone Activation.Journal of molecular biology · 2018Article
- Genetically encoded releasable photo-cross-linking strategies for studying protein-protein interactions in living cells.Nature protocols · 2017Article
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7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
HdeA and HdeB constitute the essential chaperone system that functions in the unique periplasmic space of Gram-negative enteric bacteria to confer acid resistance. How this two-chaperone machinery cooperates to protect a broad range of client proteins from acid denaturation while avoiding nonspecific binding during bacterial passage through the highly acidic human stomach remains unclear. We have developed a comparative proteomic strategy that combines the genetically encoded releasable protein photocross-linker with 2D difference gel electrophoresis, which allows an unbiased side-by-side comparison of the entire client pools from these two acid-activated chaperones in Escherichia coli Our results reveal distinct client specificities between HdeA and HdeB in vivo that are determined mainly by their different responses to pH stimulus. The intracellular acidity serves as an environmental cue to determine the folding status of both chaperones and their clients, enabling specific chaperone-client binding and release under defined pH conditions. This cooperative and synergistic mode of action provides an efficient, economical, flexible, and finely tuned protein quality control strategy for coping with acid stress.
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