ArticleGenes & development2004
A chaperone network controls the heat shock response in E. coli.
Article in Genes & development, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
96 citing papers in PubMed, 210 citations in OpenAlex.
- Proteomic Profiling Reveals Intracellular Regulatory Network Disturbance Induced by QseB Deletion inMicroorganisms · 2026Article
- Synergies and trade-offs in the heat shock response mechanism.PLoS computational biology · 2026Article
- Cell-selective multiplexed bioorthogonal noncanonical amino acid tagging for nascent proteomics.Nature chemical biology · 2026Article
- Article
- Nucleoid-associated proteins: molecular mechanisms in microbial adaptation.World journal of microbiology & biotechnology · 2025Review
- Peering into the Bacterial Cell: From Transcription to Functional Genomics.Journal of molecular biology · 2025Review
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Physical communication pathways in bacteria: an extra layer to quorum sensing.Biophysical reviews · 2025Review
- Membrane-associated σ factors disrupt rRNA operon clustering in Escherichia coli.PLoS biology · 2025Article
- Targeting bacterial transcription factors for infection control: opportunities and challenges.Transcription · 2025Review
- Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis.Journal of biosciences · 2025Review
- Whole Genome Sequencing and Comparative Genomic Analysis ofMicroorganisms · 2024Article
- A simple and unified protocol to purify all seven Escherichia coli RNA polymerase sigma factors.Journal of applied genetics · 2024Article
- StressME: Unified computing framework of Escherichia coli metabolism, gene expression, and stress responses.PLoS computational biology · 2024Article
- High-throughput sequencing reveals the structure and metabolic resilience of desert microbiome confronting climate change.Frontiers in plant science · 2024Article
- Article
- Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.Biomolecules · 2023Article
- Lessons Learned from Two Decades of Modeling the Heat-Shock Response.Biomolecules · 2022Review
- DnaK response to expression of protein mutants is dependent on translation rate and stability.Communications biology · 2022Article
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
36 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The heat shock response controls levels of chaperones and proteases to ensure a proper cellular environment for protein folding. In Escherichia coli, this response is mediated by the bacterial-specific transcription factor, sigma32. The DnaK chaperone machine regulates both the amount and activity of sigma32, thereby coupling sigma32 function to the cellular protein folding state. In this manuscript, we analyze the ability of other major chaperones in E. coli to regulate sigma32, and we demonstrate that the GroEL/S chaperonin is an additional regulator of sigma32. We show that increasing the level of GroEL/S leads to a decrease in sigma32 activity in vivo and this effect can be eliminated by co-overexpression of a GroEL/S-specific substrate. We also show that depletion of GroEL/S in vivo leads to up-regulation of sigma32 by increasing the level of sigma32. In addition, we show that changing the levels of GroEL/S during stress conditions leads to measurable changes in the heat shock response. Using purified proteins, we show that that GroEL binds to sigma32 and decreases sigma32-dependent transcription in vitro, suggesting that this regulation is direct. We discuss why using a chaperone network to regulate sigma32 results in a more sensitive and accurate detection of the protein folding environment.
Indexed as
Identifiers
What OpenQuestion holds
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.