Identification of members of the HSP30 small heat shock protein family and characterization of their developmental regulation in heat-shockedxenopus laevis embryos

1995 ◽  
Vol 17 (4) ◽  
pp. 331-339 ◽  
Author(s):  
Ying Tam ◽  
John J. Heikkila
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Developmental Regulation ◽  
Small Heat Shock Protein ◽  
Protein Family

Characterization of the zebrafish small heat shock protein family

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Kimberly S Elicker ◽  
Tomoki Kurihara ◽  
Lara D Hutson
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Protein Family

scholarly journals Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family

2005 ◽  
Vol 4 (12) ◽  
pp. 1990-1997 ◽  
Author(s):  
N. de Miguel ◽  
P. C. Echeverria ◽  
S. O. Angel
Keyword(s):  
Heat Shock ◽  
Toxoplasma Gondii ◽  
Heat Shock Protein ◽  
Subcellular Localization ◽  
Small Heat Shock Protein ◽  
Terminal Segment ◽  
Protein Family ◽  
Link Type ◽  
Identification And Characterization

ABSTRACT The results of this study describe the identification and characterization of the Toxoplasma gondii α-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org ) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous α-crystallin domain, which is the key characteristic of sHsps. However, the N-terminal segment of each protein contains unique characteristics in size and sequence. Most T. gondii sHsps are constitutively expressed in tachyzoites and fully differentiated bradyzoites, with the exception of Hsp30/Bag1. Interestingly, by subcellular localization we observed that T. gondii sHsps are located in different compartments. Hsp20 is located at the apical end of the cell, Hsp28 is located inside the mitochondrion, Hsp29 showed a membrane-associated labeling, and Hsp21 appeared throughout the cytosol of the parasites. These particular differences in the immunostaining patterns suggest that their targets and functions might be different.

scholarly journals Isolation and characterization of a human heart cDNA encoding a new member of the small heat shock protein family — HSPL27

1996 ◽  
Vol 1314 (1-2) ◽  
pp. 120-124 ◽  
Author(s):  
Wai Yip Lam ◽  
Stephen Kwok Wing Tsui ◽  
Patrick Tik Wan Law ◽  
Sharon Chui Wah Luk ◽  
Kwok Pui Fung ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Heart ◽  
Small Heat Shock Protein ◽  
Protein Family ◽  
Isolation And Characterization

scholarly journals Knockdown of the small heat-shock protein p26 by RNA interference modifies the diapause proteome of Artemia franciscana

2019 ◽  
Vol 97 (4) ◽  
pp. 471-479
Author(s):  
Hajer Salem Malitan ◽  
Alejandro M. Cohen ◽  
Thomas H. MacRae
Keyword(s):  
Rna Interference ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Small Heat Shock Protein ◽  
Isotopic Labeling ◽  
Artemia Franciscana ◽  
Signal Transducers ◽  
Translation Factors

Embryos of the crustacean Artemia franciscana may arrest as gastrulae, forming cysts that enter diapause, which is a state of reduced metabolism and enhanced stress tolerance. Diapausing cysts survive physiological stresses for years due, in part, to molecular chaperones. p26, a small heat-shock protein, is an abundant diapause-specific molecular chaperone in cysts, and it affects embryo development and stress tolerance. p26 is therefore thought to influence many proteins in cysts, and this study was undertaken to determine how the loss of p26 by RNA interference (RNAi) affects the diapause proteome of A. franciscana. The proteome was analyzed by shot-gun proteomics coupled to differential isotopic labeling and tandem mass spectrometry. Proteins in the diapause proteome included metabolic enzymes, antioxidants, binding proteins, structural proteins, transporters, translation factors, receptors, and signal transducers. Proteins within the diapause proteome either disappeared or were reduced in amount when p26 was knocked down, or conversely, proteins appeared or increased in amount. Those proteins that disappeared may be p26 substrates, whereas the synthesis of those proteins that appeared or increased may be regulated by p26. This study provides the first global characterization of the diapause proteome of A. franciscana and demonstrates that the sHsp p26 influences proteome composition.

scholarly journals Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Stephen D. Weeks ◽  
Lydia K. Muranova ◽  
Michelle Heirbaut ◽  
Steven Beelen ◽  
Sergei V. Strelkov ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Motor Neuron ◽  
Small Heat Shock Protein ◽  
Motor Neuron Diseases ◽  
Hereditary Motor
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