scholarly journals Plantation Forestry under Global Warming: Hybrid Poplars with Improved Thermotolerance Provide New Insights on the in Vivo Function of Small Heat Shock Protein Chaperones

2013 ◽  
Vol 164 (2) ◽  
pp. 978-991 ◽  
Author(s):  
Irene Merino ◽  
Angela Contreras ◽  
Zhong-Ping Jing ◽  
Fernando Gallardo ◽  
Francisco M. Cánovas ◽  
...  
Keyword(s):  
Global Warming ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Plantation Forestry ◽  
Hybrid Poplars ◽  
Protein Chaperones

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.

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

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.

Expression of small heat shock protein αB-crystallin is induced after hepatic stellate cell activation

2000 ◽  
Vol 279 (6) ◽  
pp. G1333-G1342 ◽  
Author(s):  
Alon Lang ◽  
Laura W. Schrum ◽  
Robert Schoonhoven ◽  
Shmuel Tuvia ◽  
Jose A. Solís-Herruzo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hepatic Stellate Cell ◽  
Cell Activation ◽  
Stellate Cell ◽  
Small Heat Shock Protein ◽  
Immunocytochemical Staining ◽  
Αb Crystallin ◽  
Quiescent Hscs

Using the differential PCR display method to select cDNA fragments that are differentially expressed after hepatic stellate cell (HSC) activation, we have isolated from activated HSCs a cDNA that corresponds to rat αB-crystallin. Northern blots confirmed expression of αB-crystallin in culture-activated HSCs but not in quiescent HSCs. Western blot analysis and immunocytochemical staining confirmed expression of αB-crystallin protein in activated but not quiescent HSCs. αB-crystallin is induced as early as 6 h after plating HSCs on plastic and continues to be expressed for 14 days in culture. Expression of αB-crystallin was also induced in vivo in activated HSCs from experimental cholestatic liver fibrosis. Confocal microscopy demonstrated a cytoplasmic distribution of αB-crystallin in a cytoskeletal pattern. Heat shock treatment resulted in an immediate perinuclear redistribution that in time returned to a normal cytoskeletal distribution. The expression pattern of αB-crystallin was similar to that of HSP25, another small heat shock protein, but differed from the classic heat shock protein HSP70. Therefore, αB-crystallin represents an early marker for HSC activation.

scholarly journals HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells

2005 ◽  
Vol 14 (12) ◽  
pp. 1659-1669 ◽  
Author(s):  
Serena Carra ◽  
Mitchel Sivilotti ◽  
Aura T. Chávez Zobel ◽  
Herman Lambert ◽  
Jacques Landry
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cultured Cells ◽  
Neuromuscular Disorders ◽  
Small Heat Shock Protein ◽  
Chaperone Activity
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