scholarly journals hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function.

1989 ◽  
Vol 9 (11) ◽  
pp. 5265-5271 ◽  
Author(s):  
R E Susek ◽  
S L Lindquist
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mutational Analysis ◽  
Small Heat Shock Protein ◽  
Major Effect ◽  
Selfish Dna ◽  
Dna Elements ◽  
Cloned Gene ◽  
Shock Proteins

Analysis of the cloned gene confirms that hsp26 of Saccharomyces cerevisiae is a member of the small heat shock protein superfamily. Previous mutational analysis failed to demonstrate any function for the protein. Further experiments presented here demonstrate that hsp26 has no obvious regulatory role and no major effect on thermotolerance. It is possible that the small heat shock protein genes originated as primitive viral or selfish DNA elements.

hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function

1989 ◽  
Vol 9 (11) ◽  
pp. 5265-5271
Author(s):  
R E Susek ◽  
S L Lindquist
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mutational Analysis ◽  
Small Heat Shock Protein ◽  
Major Effect ◽  
Selfish Dna ◽  
Dna Elements ◽  
Cloned Gene ◽  
Shock Proteins

Analysis of the cloned gene confirms that hsp26 of Saccharomyces cerevisiae is a member of the small heat shock protein superfamily. Previous mutational analysis failed to demonstrate any function for the protein. Further experiments presented here demonstrate that hsp26 has no obvious regulatory role and no major effect on thermotolerance. It is possible that the small heat shock protein genes originated as primitive viral or selfish DNA elements.

scholarly journals Small Heat Shock Protein αA-crystallin Regulates Epithelial Sodium Channel Expression

2007 ◽  
Vol 282 (38) ◽  
pp. 28149-28156 ◽  
Author(s):  
Ossama B. Kashlan ◽  
Gunhild M. Mueller ◽  
Mohammad Z. Qamar ◽  
Paul A. Poland ◽  
Annette Ahner ◽  
...  
Keyword(s):  
Quality Control ◽  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Collecting Duct ◽  
Small Heat Shock Protein ◽  
Er Quality Control ◽  
Post Translational Modifications ◽  
Channel Expression ◽  
Shock Proteins

Integral membrane proteins are synthesized on the cytoplasmic face of the endoplasmic reticulum (ER). After being translocated or inserted into the ER, they fold and undergo post-translational modifications. Within the ER, proteins are also subjected to quality control checkpoints, during which misfolded proteins may be degraded by proteasomes via a process known as ER-associated degradation. Molecular chaperones, including the small heat shock protein αA-crystallin, have recently been shown to play a role in this process. We have now found that αA-crystallin is expressed in cultured mouse collecting duct cells, where apical Na+ transport is mediated by epithelial Na+ channels (ENaC). ENaC-mediated Na+ currents in Xenopus oocytes were reduced by co-expression of αA-crystallin. This reduction in ENaC activity reflected a decrease in the number of channels expressed at the cell surface. Furthermore, we observed that the rate of ENaC delivery to the cell surface of Xenopus oocytes was significantly reduced by co-expression of αA-crystallin, whereas the rate of channel retrieval remained unchanged. We also observed that αA-crystallin and ENaC co-immunoprecipitate. These data are consistent with the hypothesis that small heat shock proteins recognize ENaC subunits at ER quality control checkpoints and can target ENaC subunits for ER-associated degradation.

scholarly journals Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

2004 ◽  
Vol 23 (3) ◽  
pp. 638-649 ◽  
Author(s):  
Martin Haslbeck ◽  
Nathalie Braun ◽  
Thusnelda Stromer ◽  
Bettina Richter ◽  
Natascha Model ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

scholarly journals Small Heat Shock Proteins Can Confer Tolerance to Nanomaterial-induced Toxicity

HortScience ◽  
2014 ◽  
Vol 49 (8) ◽  
pp. 1116-1121 ◽  
Author(s):  
Hanseul Park ◽  
Eunhye Ko ◽  
Yeh-Jin Ahn
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Multiwalled Carbon ◽  
E Coli ◽  
Transgenic Cell ◽  
Heat Shock Cognate 70 ◽  
Leaf Tissues ◽  
Shock Proteins ◽  
Transgenic Cell Line

The expression of a small heat shock protein (sHSP) in plants and its possible function in conditions related to nanomaterial exposure were examined. Multiwalled carbon nanotubes (MWCNTs) and silver nanoparticles (AgNPs) induced toxicity that was indicated by the bending and curling of carrot leaf tissues. Both nanomaterials induced the expression of a small heat shock protein in carrot, DcHsp17.7, but reduced the level of a constitutive heat shock cognate 70. To examine the possible function of DcHsp17.7, the coding gene was heterologously expressed in Escherichia coli. Both nanomaterials reduced the viability of E. coli cell lines. However, the transgenic cell line heterologously expressing DcHsp17.7 showed higher levels of cell viability, compared with vector controls, when exposed to MWCNTs and, more notably, to AgNPs. To the best of our knowledge, this is the first study reporting the influence of nanomaterials on the expression of a plant sHSP and its possible function in conferring tolerance to nanomaterial stress.

scholarly journals The N terminus of the small heat shock protein HSPB7 drives its polyQ aggregation–suppressing activity

2019 ◽  
Vol 294 (25) ◽  
pp. 9985-9994 ◽  
Author(s):  
Di Wu ◽  
Jan J. Vonk ◽  
Felix Salles ◽  
Danara Vonk ◽  
Martin Haslbeck ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Inhibiting Activity ◽  
Aggregation Assay ◽  
The Family ◽  
Aggregation Activity ◽  
Shock Proteins ◽  
Necessary And Sufficient

Heat shock protein family B (small) member 7 (HSPB7) is a unique, relatively unexplored member within the family of human small heat shock proteins (HSPBs). Unlike most HSPB family members, HSPB7 does not oligomerize and so far has not been shown to associate with any other member of the HSPB family. Intriguingly, it was found to be the most potent member within the HSPB family to prevent aggregation of proteins with expanded polyglutamine (polyQ) stretches. How HSPB7 suppresses polyQ aggregation has remained elusive so far. Here, using several experimental strategies, including in vitro aggregation assay, immunoblotting and fluorescence approaches, we show that the polyQ aggregation-inhibiting activity of HSPB7 is fully dependent on its flexible N-terminal domain (NTD). We observed that the NTD of HSPB7 is both required for association with and inhibition of polyQ aggregation. Remarkably, replacing the NTD of HSPB1, which itself cannot suppress polyQ aggregation, with the NTD of HSPB7 resulted in a hybrid protein that gained anti-polyQ aggregation activity. The hybrid NTDHSPB7–HSPB1 protein displayed a reduction in oligomer size and, unlike WT HSPB1, associated with polyQ. However, experiments with phospho-mimicking HSPB1 mutants revealed that de-oligomerization of HSPB1 alone does not suffice to gain polyQ aggregation–inhibiting activity. Together, our results reveal that the NTD of HSPB7 is both necessary and sufficient to bind to and suppress the aggregation of polyQ-containing proteins.

scholarly journals Small heat shock proteins and neurodegeneration: recent developments

2018 ◽  
Vol 9 (1) ◽  
pp. 94-102 ◽  
Author(s):  
Nikos Kourtis ◽  
Nektarios Tavernarakis
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Neurodegenerative Diseases ◽  
Molecular Chaperones ◽  
Neurodegenerative Disorders ◽  
Critical Role ◽  
Small Heat Shock Protein ◽  
Recent Developments ◽  
Shock Proteins

AbstractMembers of the small heat shock protein (sHSP) family are molecular chaperones with a critical role in the maintenance of cellular homeostasis under unfavorable conditions. The chaperone properties of sHSPs prevent protein aggregation, and sHSP deregulation underlies the pathology of several diseases, including neurodegenerative disorders. Recent evidence suggests that the clientele of sHSPs is broad, and the mechanisms of sHSP-mediated neuroprotection diverse. Nonetheless, the crosstalk of sHSPs with the neurodegeneration-promoting signaling pathways remains poorly understood. Here, we survey recent findings on the role and regulation of sHSPs in neurodegenerative diseases.

scholarly journals Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

2020 ◽  
Vol 39 (12) ◽  
Author(s):  
Martin Haslbeck ◽  
Nathalie Braun ◽  
Thusnelda Stromer ◽  
Bettina Richter ◽  
Natascha Model ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

scholarly journals The molecular evolution of the small heat-shock proteins in plants.

Genetics ◽  
1995 ◽  
Vol 141 (2) ◽  
pp. 785-795 ◽  
Author(s):  
E R Waters
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Cellular Localization ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Gene Families ◽  
Small Heat Shock Proteins ◽  
Amino Acid Sequences ◽  
Shock Proteins

Abstract The small heat-shock proteins have undergone a tremendous diversification in plants; whereas only a single small heat-shock protein is found in fungi and many animals, over 20 different small heat-shock proteins are found in higher plants. The small heat-shock proteins in plants have diversified in both sequence and cellular localization and are encoded by at least five gene families. In the study, 44 small heat-shock protein DNA and amino acid sequences were examined, using both phylogenetic analysis and analysis of nucleotide substitution patterns to elucidate the evolutionary history of the small heat-shock proteins. The phylogenetic relationships of the small heat-shock proteins, estimated using parsimony and distance methods, reveal the gene duplication, sequence divergence and gene conversion have all played a role in the evolution of the small heat-shock proteins. Analysis of nonsynonymous substitutions and conservative and radical replacement substitutions )in relation to hydrophobicity) indicates that the small heat-shock protein gene families are evolving at different rates. This suggests that the small heat-shock proteins may have diversified in function as well as in sequence and cellular localization.

scholarly journals Crystal structure of a small heat-shock protein fromXylella fastidiosareveals a distinct high-order structure

2017 ◽  
Vol 73 (4) ◽  
pp. 222-227 ◽  
Author(s):  
Emanuella Maria Barreto Fonseca ◽  
Valéria Scorsato ◽  
Marcelo Leite dos Santos ◽  
Atilio Tomazini Júnior ◽  
Susely Ferraz Siqueira Tada ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Xylella Fastidiosa ◽  
Small Heat Shock Protein ◽  
High Order ◽  
Order Structure ◽  
High Order Structure ◽  
Square Cavity ◽  
Shock Proteins ◽  
Order Structures

Citrus variegated chlorosis is a disease that attacks economically important citrus plantations and is caused by the plant-pathogenic bacteriumXylella fastidiosa. In this work, the structure of a small heat-shock protein fromX. fastidiosa(XfsHSP17.9) is reported. The high-order structures of small heat-shock proteins from other organisms are arranged in the forms of double-disc, hollow-sphere or spherical assemblies. Unexpectedly, the structure reported here reveals a high-order architecture forming a nearly square cavity.

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