scholarly journals Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase

2007 ◽  
Vol 16 (7) ◽  
pp. 1464-1478 ◽  
Author(s):  
Emma Åhrman ◽  
Wietske Lambert ◽  
J. Andrew Aquilina ◽  
Carol V. Robinson ◽  
Cecilia Sundby Emanuelsson
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Citrate Synthase ◽  
Small Heat Shock Protein ◽  
Cross Linking ◽  
Chemical Cross Linking

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

ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana

2008 ◽  
Vol 411 (3) ◽  
pp. 605-611 ◽  
Author(s):  
Zhijun Qiu ◽  
Thomas H. MacRae
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Citrate Synthase ◽  
Sequence Similarity ◽  
Single Gene ◽  
Small Heat Shock Protein ◽  
Subtractive Hybridization ◽  
Artemia Franciscana ◽  
Induced Aggregation

Embryos of the crustacean, Artemia franciscana, undergo alternative developmental pathways, producing either larvae or encysted embryos (cysts). The cysts enter diapause, characterized by exceptionally high resistance to environmental stress, a condition thought to involve the sHSP (small heat-shock protein), p26. Subtractive hybridization has revealed another sHSP, termed ArHsp21, in diapause-destined Artemia embryos. ArHsp21 shares sequence similarity with p26 and sHSPs from other organisms, especially in the α-crystallin domain. ArHsp21 is the product of a single gene and its synthesis occurred exclusively in diapause-destined embryos. Specifically, ArHsp21 mRNA appeared 2 days post-fertilization, followed 1 day later by the protein, and then increased until embryo release at day 5. No ArHsp21 protein was detected in embryos developing directly into larvae, although there was a small amount of mRNA at 3 days post-fertilization. The protein was degraded during post-diapause development and had disappeared completely from second instar larvae. ArHsp21 formed large oligomers in encysted embryos and transformed bacteria. When purified from bacteria, ArHsp21 functioned as a molecular chaperone in vitro, preventing heat-induced aggregation of citrate synthase and reduction-driven denaturation of insulin. Sequence characteristics, synthesis patterns and functional properties demonstrate clearly that ArHsp21 is an sHSP able to chaperone other proteins and contribute to stress tolerance during diapause. As such, ArHsp21 would augment p26 chaperone activity and it may also possess novel activities that benefit Artemia embryos exposed to stress.

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
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