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 Heterologous Expression of a Carrot Small Heat Shock Protein Increased Escherichia coli Viability under Lead and Arsenic Stresses

HortScience ◽  
2013 ◽  
Vol 48 (10) ◽  
pp. 1323-1326 ◽  
Author(s):  
Joohee Lee ◽  
Yeh-Jin Ahn
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heterologous Expression ◽  
Time Course ◽  
Leaf Tissue ◽  
Small Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Lead Ion ◽  
And Function

The expression and function of DcHsp17.7, a small heat shock protein (sHSP), in carrot (Daucus carota L.) was examined under lead [Pb(II)] and arsenic (arsenate) stresses. In a time course experiment, the level of DcHsp17.7 increased in carrot leaf tissue treated with lead ions or arsenate. To examine the function of DcHsp17.7, the DcHsp17.7 gene was cloned and introduced into Escherichia coli. Heterologous expression of DcHsp17.7 was confirmed by immunoblot analysis using a polyclonal antibody raised against DcHsp17.7. Lead ion and arsenate reduced bacterial cell viability. However, transgenic E. coli with accumulated DcHsp17.7 showed higher levels of survival under both lead ion and arsenate conditions compared with the vector control. Immunoblot analysis showed that the level of heterologously expressed DcHsp17.7 decreased under lead ion conditions, but remained the same under arsenate conditions. Our results suggest that DcHsp17.7 can confer tolerances to lead and arsenic stresses.

Protective role of Mycobacterium leprae small heat-shock protein in heterologous hosts, Escherichia coli and Mycobacterium smegmatis, grown under stress

2013 ◽  
Vol 62 (7) ◽  
pp. 959-967 ◽  
Author(s):  
Jayapal Jeya Maheshwari ◽  
Kuppamuthu Dharmalingam
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mycobacterium Smegmatis ◽  
Small Heat Shock Protein ◽  
Mycobacterium Leprae ◽  
Protective Role ◽  
Low Oxygen

The aim of this study is to examine the in vivo role of a small heat-shock protein (sHsp18) from Mycobacterium leprae in the survival of heterologous recombinant hosts carrying the gene encoding this protein under different environmental conditions that are normally encountered by M. leprae during its infection of the human host. Using an Escherichia coli system where shsp18 expression is controlled by its native promoter, we show that expression of shsp18 is induced under low oxygen tension, nutrient depletion and oxidative stress, all of which reflect the natural internal environment of the granulomas where the pathogen resides for long periods. We demonstrate the in vivo chaperone activity of sHsp18 through its ability to confer survival advantage to recombinant E. coli at heat-shock temperatures. Additional evidence for the protective role of sHsp18 was obtained when Mycobacterium smegmatis harbouring a copy of shsp18 was found to multiply better in human macrophages. Furthermore, the autokinase activity of sHsp18 protein demonstrated for what is believed to be the first time in this study implies that some of the functions of sHsp18 might be controlled by the phosphorylation state of this protein. Results from this study suggest that shsp18 might be one of the factors that facilitate the survival and persistence of M. leprae under stress and autophosphorylation of sHsp18 protein could be a mechanism used by this protein to sense changes in the external environment.

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.

Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue

2017 ◽  
Vol 51 (1) ◽  
pp. 112-121 ◽  
Author(s):  
A. R. Kayumov ◽  
M. I. Bogachev ◽  
V. A. Manuvera ◽  
V. N. Lazarev ◽  
A. V. Sabantsev ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Acholeplasma Laidlawii

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.

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