Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon,Sulfolobus tokodaii strain 7

2008 ◽  
Vol 71 (2) ◽  
pp. 771-782 ◽  
Author(s):  
Hitoshi Saji ◽  
Ryo Iizuka ◽  
Takao Yoshida ◽  
Tetsuya Abe ◽  
Shun-ichi Kidokoro ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Sulfolobus Tokodaii ◽  
And Function

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

scholarly journals Role of the Conserved SRLFDQFFG Region of α-Crystallin, a Small Heat Shock Protein

2003 ◽  
Vol 278 (51) ◽  
pp. 51159-51166 ◽  
Author(s):  
Saloni Yatin Pasta ◽  
Bakthisaran Raman ◽  
Tangirala Ramakrishna ◽  
Ch. Mohan Rao
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

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 Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity

2014 ◽  
Vol 80 (10) ◽  
pp. 2973-2980 ◽  
Author(s):  
Magali Maitre ◽  
Stéphanie Weidmann ◽  
Florence Dubois-Brissonnet ◽  
Vanessa David ◽  
Jacques Covès ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Phospholipid Composition ◽  
Small Heat Shock Protein ◽  
Oenococcus Oeni ◽  
Lipid Binding ◽  
Phospholipid Content ◽  
Ethanol Stress ◽  
Content Type

ABSTRACTMalolactic fermentation in wine is often carried out byOenococcus oeni. Wine is a stressful environment for bacteria because ethanol is a toxic compound that impairs the integrity of bacterial membranes. The small heat shock protein (sHsp) Lo18 is an essential actor of the stress response inO. oeni. Lo18 prevents the thermal aggregation of proteins and plays a crucial role in membrane quality control. Here, we investigated the interaction between Lo18 and four types of liposomes: one was prepared fromO. oenigrown under optimal growth conditions (here, control liposomes), one was prepared fromO. oenigrown in the presence of 8% ethanol (here, ethanol liposomes), one was prepared from synthetic phospholipids, and one was prepared from phospholipids fromBacillus subtilisorLactococcus lactis. We observed the strongest interaction between Lo18 and control liposomes. The lipid binding activity of Lo18 required the dissociation of oligomeric structures into dimers. Protein protection experiments carried out in the presence of the liposomes fromO. oenisuggested that Lo18 had a higher affinity for control liposomes than for a model protein. In anisotropy experiments, we mimicked ethanol action by temperature-dependent fluidization of the liposomes. Results suggest that the principal determinant of Lo18-membrane interaction is lipid bilayer phase behavior rather than phospholipid composition. We suggest a model to describe the ethanol adaptation ofO. oeni. This model highlights the dual role of Lo18 in the protection of proteins from aggregation and membrane stabilization and suggests how modifications of phospholipid content may be a key factor determining the balance between these two functions.

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.

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