scholarly journals Interaction of ATP with a Small Heat Shock Protein from Mycobacterium leprae: Effect on Its Structure and Function

2015 ◽  
Vol 9 (3) ◽  
pp. e0003661 ◽  
Author(s):  
Sandip Kumar Nandi ◽  
Ayon Chakraborty ◽  
Alok Kumar Panda ◽  
Sougata Sinha Ray ◽  
Rajiv Kumar Kar ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Mycobacterium Leprae ◽  
Structure And Function ◽  
And Function

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 A Cytosolic Heat Shock Protein Expressed in Carrot (Daucus carota L.) Enhances Cell Viability under Oxidative and Osmotic Stress Conditions

HortScience ◽  
2012 ◽  
Vol 47 (1) ◽  
pp. 143-148 ◽  
Author(s):  
Yeh-Jin Ahn ◽  
Na-Hyun Song
Keyword(s):  
Heat Shock ◽  
Osmotic Stress ◽  
Heat Shock Protein ◽  
Cell Viability ◽  
Daucus Carota ◽  
Leaf Tissue ◽  
Small Heat Shock Protein ◽  
Stress Conditions ◽  
Daucus Carota L ◽  
And Function

The expression and function of DcHsp17.7, a small heat shock protein expressed in carrot (Daucus carota L.), was examined under oxidative and osmotic stress conditions. Comparative analysis revealed that DcHsp17.7 is a cytosolic Class I protein. Sequence alignment showed that DcHsp17.7 has the characteristic α-crystalline domain-containing consensus regions I and II. Under oxidative [hydrogen peroxide (H2O2)] and osmotic (polyethylene glycol) stress conditions, DcHsp17.7 accumulated in carrot leaf tissue. To examine its function under these abiotic stress conditions, the coding sequence of DcHsp17.7 was introduced into Escherichia coli and expressed by isopropyl β-D-1-thiogalactopyranoside treatment. Under both oxidative and osmotic stress conditions, heterologously expressed DcHsp17.7 enhanced bacterial cell viability. The expression level of soluble proteins was higher in transgenic cells expressing DcHsp17.7 when compared with controls under these stress conditions. These results suggest that DcHsp17.7 confers tolerance to both oxidative and osmotic stresses and thereby functions as a molecular chaperone during the stresses examined.

scholarly journals Hsp22 Deficiency Induces Age-Dependent Cardiac Dilation and Dysfunction by Impairing Autophagy, Metabolism, and Oxidative Response

Antioxidants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1550
Author(s):  
Wenqian Wu ◽  
Xiaonan Sun ◽  
Xiaomeng Shi ◽  
Lo Lai ◽  
Charles Wang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Essential Role ◽  
Early Stage ◽  
Small Heat Shock Protein ◽  
Vital Role ◽  
Physiological Conditions ◽  
Age Related ◽  
And Function ◽  
Heat Shock Protein 22

Heat shock protein 22 (Hsp22) is a small heat shock protein predominantly expressed in skeletal and cardiac muscle. Previous studies indicate that Hsp22 plays a vital role in protecting the heart against cardiac stress. However, the essential role of Hsp22 in the heart under physiological conditions remains largely unknown. In this study, we used an Hsp22 knockout (KO) mouse model to determine whether loss of Hsp22 impairs cardiac growth and function with increasing age under physiological conditions. Cardiac structural and functional alterations at baseline were measured using echocardiography and invasive catheterization in Hsp22 KO mice during aging transition compared to their age-matched wild-type (WT) littermates. Our results showed that Hsp22 deletion induced progressive cardiac dilation along with declined function during the aging transition. Mechanistically, the loss of Hsp22 impaired BCL-2–associated athanogene 3 (BAG3) expression and its associated cardiac autophagy, undermined cardiac energy metabolism homeostasis and increased oxidative damage. This study showed that Hsp22 played an essential role in the non-stressed heart during the early stage of aging, which may bring new insight into understanding the pathogenesis of age-related dilated cardiomyopathy.

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