scholarly journals DcHsp17.7, a Small Heat Shock Protein from Carrot, Is Upregulated under Cold Stress and Enhances Cold Tolerance by Functioning as a Molecular Chaperone

HortScience ◽  
2010 ◽  
Vol 45 (3) ◽  
pp. 469-474 ◽  
Author(s):  
Na-Hyun Song ◽  
Yeh-Jin Ahn
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Stress ◽  
Cold Tolerance ◽  
Functional Properties ◽  
Molecular Chaperone ◽  
Small Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Transformed Cells ◽  
E Coli

The expression profile and functional properties of DcHsp17.7, a small heat shock protein from carrot (Daucus carota L.), were examined under cold stress. Immunoblot analysis showed that low temperature (2 °C) induced DcHsp17.7 in vegetative tissues. Differential accumulation of the transcript and protein under the cold suggests that expression of DcHsp17.7 might be controlled at the transcriptional and/or translational levels. To examine the functional properties of DcHsp17.7, the gene was expressed in Escherichia coli. When exposed to 2 °C for 10 days, transformed cells expressing DcHsp17.7 showed 115% cell viability, whereas control cells recorded 24%, suggesting that DcHsp17.7 can confer cold tolerance. The amount of soluble protein under the cold was 83% in transformed cells expressing DcHsp17.7, whereas the control cells showed only 52%, suggesting that DcHsp17.7 functions as a molecular chaperone preventing cold-induced protein degradation. Native-polyacrylamide analysis revealed that DcHsp17.7 was found in two oligomeric complexes (≈160 and 240 kDa) and possibly multiple complexes (from 300 to 450 kDa) in cold-stressed carrot and transformed E. coli, respectively. During prolonged cold stress, these complexes disappeared and then reappeared, suggesting that the dissociation and reassociation of DcHsp17.7 complexes might be important for the function of the protein.

scholarly journals Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus

2001 ◽  
Vol 183 (17) ◽  
pp. 5198-5202 ◽  
Author(s):  
Pongpan Laksanalamai ◽  
Dennis L. Maeder ◽  
Frank T. Robb
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mechanism Of Action ◽  
Pyrococcus Furiosus ◽  
Small Heat Shock Protein ◽  
Control Culture ◽  
Gene Encoding ◽  
E Coli

ABSTRACT The small heat shock protein (sHSP) from the hyperthermophilePyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. colioverexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

scholarly journals Expression of a Gene Encoding the Carrot HSP17.7 in Escherichia coli Enhances Cell Viability and Protein Solubility Under Heat Stress

HortScience ◽  
2009 ◽  
Vol 44 (3) ◽  
pp. 866-869 ◽  
Author(s):  
Hyesoon Kim ◽  
Yeh-Jin Ahn
Keyword(s):  
Escherichia Coli ◽  
Heat Stress ◽  
Protein Solubility ◽  
Small Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Transformed Cells ◽  
Bacterial Cells ◽  
Native Page ◽  
E Coli ◽  
Inducible Protein

DcHSP17.7, a small heat shock protein from carrot (Daucus carota L.), was expressed in Escherichia coli to examine its functional mechanism under heat stress. When transformed cells expressing DcHSP17.7 were exposed to 50 °C for 1 h, the number of viable cells was ≈4-fold higher than that of control. When the amount of soluble proteins was compared, it was more than twofold higher in transformed cells expressing DcHSP17.7 than that in control, suggesting that DcHSP17.7 may function as a molecular chaperone preventing heat-inducible protein degradation. Native-PAGE followed by immunoblot analysis showed that in transformed E. coli, DcHSP17.7 was present in an oligomeric complex, ≈300 kDa in molecular mass, on isopropyl b-D-thiogalactopyranoside treatment. However, the complex rapidly disappeared when bacterial cells were exposed to heat stress. In carrot, DcHSP17.7 was found in the similar-sized complex (≈300 kDa), but only during heat stress (40 °C), suggesting that the functional structure of DcHSP17.7 may be different in transformed E. coli from that in carrot.

scholarly journals Small heat shock protein Hsp67Bc plays a significant role in Drosophila melanogaster cold stress tolerance

2020 ◽  
Vol 223 (21) ◽  
pp. jeb219592
Author(s):  
Dina Malkeyeva ◽  
Elena Kiseleva ◽  
Svetlana Fedorova
Keyword(s):  
Drosophila Melanogaster ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Stress ◽  
Stress Tolerance ◽  
Developmental Stages ◽  
Small Heat Shock Protein ◽  
Recovery Phase ◽  
Main Function

ABSTRACTHsp67Bc in Drosophila melanogaster is a member of the small heat shock protein family, the main function of which is to prevent the aggregation of misfolded or damaged proteins. Hsp67Bc interacts with Starvin and Hsp23, which are known to be a part of the cold stress response in the fly during the recovery phase. In this study, we investigated the role of the Hsp67Bc gene in the cold stress response. We showed that in adult Drosophila, Hsp67Bc expression increases after cold stress and decreases after 1.5 h of recovery, indicating the involvement of Hsp67Bc in short-term stress recovery. We also implemented a deletion in the D. melanogaster Hsp67Bc gene using imprecise excision of a P-element, and analysed the cold tolerance of Hsp67Bc-null mutants at different developmental stages. We found that Hsp67Bc-null homozygous flies are viable and fertile but display varying cold stress tolerance throughout the stages of ontogenesis: the survival after cold stress is slightly impaired in late third instar larvae, unaffected in pupae, and notably affected in adult females. Moreover, the recovery from chill coma is delayed in Hsp67Bc-null adults of both sexes. In addition, the deletion in the Hsp67Bc gene caused more prominent up-regulation of Hsp70 following cold stress, suggesting the involvement of Hsp70 in compensation of the lack of the Hsp67Bc protein. Taken together, our results suggest that Hsp67Bc is involved in the recovery of flies from a comatose state and contributes to the protection of the fruit fly from cold stress.

scholarly journals Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia coli Viability under Heat and Cold Stress

1999 ◽  
Vol 120 (2) ◽  
pp. 521-528 ◽  
Author(s):  
Alvaro Soto ◽  
Isabel Allona ◽  
Carmen Collada ◽  
Maria-Angeles Guevara ◽  
Rosa Casado ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Stress ◽  
Heterologous Expression ◽  
Small Heat Shock Protein ◽  
Heat And Cold Stress

scholarly journals Small Heat Shock Proteins Can Confer Tolerance to Nanomaterial-induced Toxicity

HortScience ◽  
2014 ◽  
Vol 49 (8) ◽  
pp. 1116-1121 ◽  
Author(s):  
Hanseul Park ◽  
Eunhye Ko ◽  
Yeh-Jin Ahn
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Multiwalled Carbon ◽  
E Coli ◽  
Transgenic Cell ◽  
Heat Shock Cognate 70 ◽  
Leaf Tissues ◽  
Shock Proteins ◽  
Transgenic Cell Line

The expression of a small heat shock protein (sHSP) in plants and its possible function in conditions related to nanomaterial exposure were examined. Multiwalled carbon nanotubes (MWCNTs) and silver nanoparticles (AgNPs) induced toxicity that was indicated by the bending and curling of carrot leaf tissues. Both nanomaterials induced the expression of a small heat shock protein in carrot, DcHsp17.7, but reduced the level of a constitutive heat shock cognate 70. To examine the possible function of DcHsp17.7, the coding gene was heterologously expressed in Escherichia coli. Both nanomaterials reduced the viability of E. coli cell lines. However, the transgenic cell line heterologously expressing DcHsp17.7 showed higher levels of cell viability, compared with vector controls, when exposed to MWCNTs and, more notably, to AgNPs. To the best of our knowledge, this is the first study reporting the influence of nanomaterials on the expression of a plant sHSP and its possible function in conferring tolerance to nanomaterial stress.

Sign in / Sign up

Export Citation Format

Share Document