The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25

1998 ◽  
Vol 22 (3-4) ◽  
pp. 163-173 ◽  
Author(s):  
Anton Zavialov ◽  
Rainer Benndorf ◽  
Monika Ehrnsperger ◽  
Vladimir Zav’yalov ◽  
Igor Dudich ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Functional Properties ◽  
Disulfide Bond ◽  
Small Heat Shock Protein ◽  
Structural And Functional Properties

scholarly journals DcHsp17.7, a Small Heat Shock Protein from Carrot, Is Upregulated under Cold Stress and Enhances Cold Tolerance by Functioning as a Molecular Chaperone

HortScience ◽  
2010 ◽  
Vol 45 (3) ◽  
pp. 469-474 ◽  
Author(s):  
Na-Hyun Song ◽  
Yeh-Jin Ahn
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Stress ◽  
Cold Tolerance ◽  
Functional Properties ◽  
Molecular Chaperone ◽  
Small Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Transformed Cells ◽  
E Coli

The expression profile and functional properties of DcHsp17.7, a small heat shock protein from carrot (Daucus carota L.), were examined under cold stress. Immunoblot analysis showed that low temperature (2 °C) induced DcHsp17.7 in vegetative tissues. Differential accumulation of the transcript and protein under the cold suggests that expression of DcHsp17.7 might be controlled at the transcriptional and/or translational levels. To examine the functional properties of DcHsp17.7, the gene was expressed in Escherichia coli. When exposed to 2 °C for 10 days, transformed cells expressing DcHsp17.7 showed 115% cell viability, whereas control cells recorded 24%, suggesting that DcHsp17.7 can confer cold tolerance. The amount of soluble protein under the cold was 83% in transformed cells expressing DcHsp17.7, whereas the control cells showed only 52%, suggesting that DcHsp17.7 functions as a molecular chaperone preventing cold-induced protein degradation. Native-polyacrylamide analysis revealed that DcHsp17.7 was found in two oligomeric complexes (≈160 and 240 kDa) and possibly multiple complexes (from 300 to 450 kDa) in cold-stressed carrot and transformed E. coli, respectively. During prolonged cold stress, these complexes disappeared and then reappeared, suggesting that the dissociation and reassociation of DcHsp17.7 complexes might be important for the function of the protein.

Mutant small heat shock protein B3 causes motor neuropathy: Utility of a candidate gene approach

Neurology ◽  
2010 ◽  
Vol 74 (6) ◽  
pp. 502-506 ◽  
Author(s):  
S. J. Kolb ◽  
P. J. Snyder ◽  
E. J. Poi ◽  
E. A. Renard ◽  
A. Bartlett ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Candidate Gene ◽  
Small Heat Shock Protein ◽  
Candidate Gene Approach ◽  
Motor Neuropathy

Evolution and functional diversification of the small heat shock protein/α-crystallin family in higher plants

Planta ◽  
2011 ◽  
Vol 235 (6) ◽  
pp. 1299-1313 ◽  
Author(s):  
Hernán Gabriel Bondino ◽  
Estela Marta Valle ◽  
Arjen ten Have
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Functional Diversification

The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin

2003 ◽  
Vol 111 (1) ◽  
pp. 152-157 ◽  
Author(s):  
Deron J Tessier ◽  
Padmini Komalavilas ◽  
Alyssa Panitch ◽  
Lokesh Joshi ◽  
Colleen M Brophy
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Cross Linking
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