scholarly journals Characterization of Hspb8 in Zebrafish

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1562
Author(s):  
Magda Dubińska-Magiera ◽  
Joanna Niedbalska-Tarnowska ◽  
Marta Migocka-Patrzałek ◽  
Ewelina Posyniak ◽  
Małgorzata Daczewska
Keyword(s):  
Heat Shock ◽  
Small Heat Shock Protein ◽  
Zebrafish Embryos ◽  
Gene Encoding ◽  
Tissue Integrity ◽  
Pathological Conditions ◽  
Muscle Ultrastructure ◽  
Specific Localization ◽  
Potential Use

Hspb8 is a member of the small heat shock protein (sHSP) family. Its expression is known to be upregulated under heat shock. This protein interacts with different partners and can, therefore, be involved in various processes relevant to tissue integrity and functioning. In humans, mutations in the gene encoding Hspb8 can lead to the development of various diseases such as myopathies and neuropathies. In our study, we aimed to perform an in-depth characterization of zebrafish Hspb8 during zebrafish development. We applied techniques such as RT-qPCR, Western blot, immunofluorescence, co-immunoprecipitation, LC-MS, and morpholino-mediated knockdown. We broadened the knowledge regarding zebrafish hspb8 expression during development under normal and heat shock conditions as well as its tissue- and subcellular-specific localization. A co-IP analysis allowed us to conclude that zebrafish Hspb8 can interact with proteins such as Bag3 and Hsc70, which are crucial for formation of an autophagy-inducing complex. We also demonstrated that hspb8 morpholino-mediated knockdown has an impact on zebrafish embryos’ morphology, muscle ultrastructure, and motility behavior. Our research provides a valuable resource for the potential use of the zebrafish as a model for studying pathological conditions associated with hspb8 disorders.

scholarly journals Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus

2005 ◽  
Vol 187 (15) ◽  
pp. 5236-5241 ◽  
Author(s):  
Mieko Otani ◽  
Toshiyuki Ueki ◽  
Satoshi Kozuka ◽  
Miki Segawa ◽  
Keiji Sano ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Myxococcus Xanthus ◽  
Small Heat Shock Protein ◽  
Insertion Mutation ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
2D Gel ◽  
Shock Proteins

ABSTRACT A number of heat shock proteins in Myxococcus xanthus were previously identified by two-dimensional (2D) gel electrophoresis. One of these protein was termed Mx Hsp16.6, and the gene encoding Mx Hsp16.6 was isolated. Mx Hsp16.6 consists of 147 amino acid residues and has an estimated molecular weight of 16,642, in accordance with the apparent molecular mass in the 2D gel. An α-crystallin domain, typically conserved in small heat shock proteins, was found in Mx Hsp16.6. Mx Hsp16.6 was not detected during normal vegetative growth but was immediately induced after heat shock. Expression of the hsp16.6 gene was not induced by other stresses, such as starvation, oxidation, and high osmolarity. Mx Hsp16.6 was mostly localized in particles formed after heat shock and precipitated by low-speed centrifugation. Furthermore, Mx Hsp16.6 was detected in highly electron-dense particles in heat-shocked cells by immunoelectron microscopy, suggesting that it forms large complexes with heat-denatured proteins. An insertion mutation in the hsp16.6 gene resulted in lower viability during heat shock and lower acquired thermotolerance. Therefore, it is likely that Mx Hsp16.6 plays critical roles in the heat shock response in M. xanthus.

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 DNA sequence and transcript mapping of a soybean gene encoding a small heat shock protein

1985 ◽  
Vol 82 (11) ◽  
pp. 3726-3730 ◽  
Author(s):  
E. Czarnecka ◽  
W. B. Gurley ◽  
R. T. Nagao ◽  
L. A. Mosquera ◽  
J. L. Key
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Dna Sequence ◽  
Small Heat Shock Protein ◽  
Transcript Mapping ◽  
Gene Encoding ◽  
Soybean Gene

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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