scholarly journals The Chloroplast Small Heat-Shock Protein Oligomer Is Not Phosphorylated and Does Not Dissociate during Heat Stress in Vivo

1998 ◽  
Vol 116 (3) ◽  
pp. 1151-1161 ◽  
Author(s):  
Teri Chizue Suzuki ◽  
Denise C. Krawitz ◽  
Elizabeth Vierling
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

Association of αB-Crystallin, a Small Heat Shock Protein, with Actin: Role in Modulating Actin Filament Dynamics in Vivo

2007 ◽  
Vol 366 (3) ◽  
pp. 756-767 ◽  
Author(s):  
Bhairab N. Singh ◽  
K. Sridhar Rao ◽  
Tangirala Ramakrishna ◽  
Nandini Rangaraj ◽  
Ch. Mohan Rao
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Actin Filament ◽  
Small Heat Shock Protein ◽  
Filament Dynamics ◽  
Αb Crystallin

scholarly journals Expression and Localization Patterns of a Small Heat Shock Protein that Interacts with the Helicase Domain of Cucumber Green Mottle Mosaic Virus

2019 ◽  
Vol 109 (9) ◽  
pp. 1648-1657
Author(s):  
Shanshan Liu ◽  
Lifeng Liu ◽  
Miguel A. Aranda ◽  
Bin Peng ◽  
Qinsheng Gu
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Mosaic Virus ◽  
Defense Mechanisms ◽  
Citrullus Lanatus ◽  
Small Heat Shock Protein ◽  
Helicase Domain ◽  
Rna Accumulation

Cucumber green mottle mosaic virus (CGMMV), a member of the genus Tobamovirus (family Virgaviridae), is an economically important virus that has detrimental effects on cucurbit crops worldwide. Understanding the interaction between host factors and CGMMV viral proteins will facilitate the design of new strategies for disease control. In this study, a yeast two-hybrid assay revealed that the CGMMV helicase (HEL) domain interacts with a Citrullus lanatus small heat shock protein (sHSP), and we verified this observation by performing in vitro GST pull-down and in vivo coimmunoprecipitation assays. Measurement of the levels of accumulated sHSP transcript revealed that sHSP is upregulated on initial CGMMV infection in both Nicotiana benthamiana and C. lanatus plants, although not in the systemically infected leaves. We also found that the subcellular localization of the sHSP was altered after CGMMV infection. To further validate the role of sHSP in CGMMV infection, we produced and assayed N. benthamiana transgenic plants with up- and down-regulated sHSP expression. Overexpression of sHSP inhibited viral RNA accumulation and retarded disease development, whereas sHSP silencing had no marked effect on CGMMV infection. Therefore, we postulate that the identified sHSP may be one of the factors modulating host defense mechanisms in response to CGMMV infection and that the HEL domain interaction may inhibit this sHSP function to promote viral infection.

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.

Formation of non-toxic Aβ fibrils by small heat shock protein under heat-stress conditions

2013 ◽  
Vol 430 (4) ◽  
pp. 1259-1264 ◽  
Author(s):  
Masafumi Sakono ◽  
Arata Utsumi ◽  
Tamotsu Zako ◽  
Tetsuya Abe ◽  
Masafumi Yohda ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Stress Conditions ◽  
Aβ Fibrils

scholarly journals Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo

2014 ◽  
Vol 11 (3) ◽  
pp. 2276-2284 ◽  
Author(s):  
HONGBO CHEN ◽  
ABDELNASIR ADAM ◽  
YANFEN CHENG ◽  
SHU TANG ◽  
JÖRG HARTUNG ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Cell Damage ◽  
Myocardial Cell ◽  
Myocardial Cell Damage
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