ArticleProceedings of the National Academy of Sciences of the United States of America1997
Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 138 citations in OpenAlex.
- Toward a systems metabolic engineering approach to improve thermotolerance of Escherichia coli.Microbial cell factories · 2026Review
- 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
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- 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
- In Vivo, High-Throughput Selection of Thermostable Cyclohexanone Monooxygenase (CHMO).Catalysts (Basel, Switzerland) · 2020Article
- A class I cytosolic HSP20 of rice enhances heat and salt tolerance in different organisms.Scientific reports · 2020Article
- Silencing of class I small heat shock proteins affects seed-related attributes and thermotolerance in rice seedlings.Planta · 2019Article
- In a quest for engineering acidophiles for biomining applications: challenges and opportunities.Genes · 2018Review
- Heterogeneous expression of DnaK gene from Alicyclobacillus acidoterrestris improves the resistance of Escherichia coli against heat and acid stress.AMB Express · 2017Article
- A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σScientific reports · 2017Article
- Identification and characterization of the GhHsp20 gene family in Gossypium hirsutum.Scientific reports · 2016Article
- Characterization of rice small heat shock proteins targeted to different cellular organelles.Cell stress & chaperones · 2015Article
- A novel mechanism for small heat shock proteins to function as molecular chaperones.Scientific reports · 2015Article
- Expression of a gene encoding a rice RING zinc-finger protein, OsRZFP34, enhances stomata opening.Plant molecular biology · 2014Article
- A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity.Journal of bacteriology · 2014Article
- Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins.Protein science : a publication of the Protein Society · 2014Article
- In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-cross-linker.The Journal of biological chemistry · 2013Article
- ZmHSP16.9, a cytosolic class I small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco.Plant cell reports · 2012Article
- Proteomics of rice in response to heat stress and advances in genetic engineering for heat tolerance in rice.Plant cell reports · 2011Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A gene encoding the rice 16.9-kDa class I low-molecular-mass (LMM) heat-shock protein (HSP), Oshsp16.9, was introduced into Escherichia coli using the pGEX-2T expression vector to analyze the possible function of this LMM HSP under heat stress. It is known that E. coli does not normally produce class I LMM HSPs. We compared the survivability of E. coli XL1-Blue cells transformed with a recombinant plasmid containing a glutathione S-transferase (GST)-Oshsp16.9 fusion protein (pGST-FL cells) with the control E. coli cells transformed with the pGEX-2T vector (pGST cells) under heat-shock (HS) after isopropyl beta-D-thiogalactopyranoside induction. The pGST-FL cells demonstrated thermotolerance at 47.5 degrees C, a treatment that was lethal to the pGST cells. When the cell lysates from these two E. coli transformants were heated at 55 degrees C, the amount of protein denatured in the pGST-FL cells was 50% less than that of the pGST cells. Similar results as pGST-FL cells were obtained in pGST-N78 cells (cells produced a fusion protein with only the N-terminal 78 aa in the Oshsp16.9 portion) but not in pGST-C108 cells (cells produced a fusion protein with C-terminal 108 aa in the Oshsp16.9 portion). The acquired thermotolerant pGST-FL cells synthesized three types of HSPs, including the 76-, 73-, and 64-kDa proteins according to their abundance at a lethal temperature of 47.5 degrees C. This finding indicates that a plant class I LMM HSP, when effectively expressed in transformed prokaryotic cells that do not normally synthesize this class of LMM HSPs, may directly or indirectly increase thermotolerance.
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