ArticleJournal of bacteriology2014
A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 51 citations in OpenAlex.
- Enhancement of heat resistance ofEngineering microbiology · 2026Article
- Toward a systems metabolic engineering approach to improve thermotolerance of Escherichia coli.Microbial cell factories · 2026Review
- Earth's Climate History Explains Life's Temperature Optima.Ecology and evolution · 2024Article
- Effects of small heat shock proteins from thermotolerant bacteria on the stress resistance of Escherichia coli to temperature, pH, and hyperosmolarity.Extremophiles : life under extreme conditions · 2024Article
- Integration of (S)-2,3-oxidosqualene enables E. coli to become Iron Man E. coli with improved overall tolerance.Biotechnology for biofuels and bioproducts · 2023Article
- Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space.Nature cell biology · 2023Article
- Surface display of carbonic anhydrase onSynthetic and systems biotechnology · 2022Article
- The Caenorhabditis elegans 12-kDa small heat shock proteins with little in vitro chaperone activity play crucial roles for its dauer formation, longevity, and reproduction.Protein science : a publication of the Protein Society · 2021Article
- The N-terminal MYB domains affect the stability and folding aspects of Arabidopsis thaliana MYB4 transcription factor under thermal stress.Protoplasma · 2021Article
- Comparative transcriptome analyses revealed different heat stress responses in pigeonpea (Cajanus cajan) and its crop wild relatives.Plant cell reports · 2021Article
- Impact of the Resistance Responses to Stress Conditions Encountered in Food and Food Processing Environments on the Virulence and Growth Fitness of Non-TyphoidalFoods (Basel, Switzerland) · 2021Review
- Post-Transcriptional Regulation of RseA by Small RNAs RyhB and FnrS inFrontiers in molecular biosciences · 2021Article
- Identification and Characterization of the Small Heat Shock Protein Hsp20 from Oenococcus oeni SD-2a.Current microbiology · 2020Article
- IbpB-bound substrate release in living cells as revealed by unnatural amino acid-mediated photo-crosslinking.FEBS open bio · 2020Article
- The noncanonical small heat shock protein HSP-17 fromThe Journal of biological chemistry · 2020Article
- Improving stress tolerance and cell integrity of Rhodococcus ruber by overexpressing small-shock-protein Hsp16 of Rhodococcus.Journal of industrial microbiology & biotechnology · 2018Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- In a quest for engineering acidophiles for biomining applications: challenges and opportunities.Genes · 2018Review
- Expression of CeHSP17 Protein in Response to Heat Shock and Heavy Metal Ions.Journal of nematology · 2017Article
- A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σScientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is essential for organisms to adapt to fluctuating growth temperatures. Escherichia coli, a model bacterium commonly used in research and industry, has been reported to grow at a temperature lower than 46.5°C. Here we report that the heterologous expression of the 17-kDa small heat shock protein from the nematode Caenorhabditis elegans, CeHSP17, enables E. coli cells to grow at 50°C, which is their highest growth temperature ever reported. Strikingly, CeHSP17 also rescues the thermal lethality of an E. coli mutant deficient in degP, which encodes a protein quality control factor localized in the periplasmic space. Mechanistically, we show that CeHSP17 is partially localized in the periplasmic space and associated with the inner membrane of E. coli, and it helps to maintain the cell envelope integrity of the E. coli cells at the lethal temperatures. Together, our data indicate that maintaining the cell envelope integrity is crucial for the E. coli cells to grow at high temperatures and also shed new light on the development of thermophilic bacteria for industrial application.
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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.