ArticleThe Journal of biological chemistry2016
Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 46 citations in OpenAlex.
- A Narrative Review of the Role of S-Glutathionylation in Bacteria.Microorganisms · 2025Review
- SMR peptide antagonizesMicrobiology spectrum · 2024Article
- Ancestors in the Extreme: A Genomics View of Microbial Diversity in Hypersaline Aquatic Environments.Results and problems in cell differentiation · 2024Article
- Gbb glutathionylation promotes its proteasome-mediated degradation to inhibit synapse growth.The Journal of cell biology · 2023Article
- Effect of evolution of the C-terminal region on chaperone activity of Hsp70.Protein science : a publication of the Protein Society · 2023Article
- From guide to guard-activation mechanism of the stress-sensing chaperone Get3.Molecular cell · 2022Article
- Hsp70 in Redox Homeostasis.Cells · 2022Review
- Article
- Dodecin as carrier protein for immunizations and bioengineering applications.Scientific reports · 2020Article
- Article
- Dysregulation of the glutaredoxin/American journal of physiology. Cell physiology · 2020Article
- Identification of Functional Interactome of Colistin Resistance Protein MCR-1 inFrontiers in microbiology · 2020Article
- The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast.The Journal of biological chemistry · 2018Article
- Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry.Journal of visualized experiments : JoVE · 2018Article
- A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Disrupted Hydrogen-Bond Network and Impaired ATPase Activity in an Hsc70 Cysteine Mutant.Biochemistry · 2018Article
- A conserved R type Methionine Sulfoxide Reductase reverses oxidized GrpEL1/Mge1 to regulate Hsp70 chaperone cycle.Scientific reports · 2018Article
- Maintaining a Healthy Proteome during Oxidative Stress.Molecular cell · 2018Review
- Article
- A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Journal of molecular biology · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DnaK is the major bacterial Hsp70, participating in DNA replication, protein folding, and the stress response. DnaK cooperates with the Hsp40 co-chaperone DnaJ and the nucleotide exchange factor GrpE. Under non-stress conditions, DnaK binds to the heat shock transcription factor σ(32)and facilitates its degradation. Oxidative stress results in temporary inactivation of DnaK due to depletion of cellular ATP and thiol modifications such as glutathionylation until normal cellular ATP levels and a reducing environment are restored. However, the biological significance of DnaK glutathionylation remains unknown, and the mechanisms by which glutathionylation may regulate the activity of DnaK are also unclear. We investigated the conditions under which Escherichia coli DnaK undergoesS-glutathionylation. We observed glutathionylation of DnaK in lysates of E. coli cells that had been subjected to oxidative stress. We also obtained homogeneously glutathionylated DnaK using purified DnaK in the apo state. We found that glutathionylation of DnaK reversibly changes the secondary structure and tertiary conformation, leading to reduced nucleotide and peptide binding ability. The chaperone activity of DnaK was reversibly down-regulated by glutathionylation, accompanying the structural changes. We found that interaction of DnaK with DnaJ, GrpE, or σ(32)becomes weaker when DnaK is glutathionylated, and the interaction is restored upon deglutathionylation. This study confirms that glutathionylation down-regulates the functions of DnaK under oxidizing conditions, and this down-regulation may facilitate release of σ(32)from its interaction with DnaK, thus triggering the heat shock response. Such a mechanism provides a link between oxidative stress and the heat shock response in bacteria.
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