The Caenorhabditis elegans 12‐kDa small heat shock proteins with little in vitro chaperone activity play crucial roles for its dauer formation, longevity and reproduction

2021 ◽  
Author(s):  
Xinmiao Fu ◽  
Anastasia N Ezemaduka ◽  
Xinping Lu ◽  
Zengyi Chang
Keyword(s):  
Caenorhabditis Elegans ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Chaperone Activity ◽  
Dauer Formation ◽  
Shock Proteins

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

Translation of Some Maize Small Heat Shock Proteins Is Initiated From Internal In-Frame AUGs

Genetics ◽  
1998 ◽  
Vol 148 (1) ◽  
pp. 471-477
Author(s):  
J Roger H Frappier ◽  
David B Walden ◽  
Burr G Atkinson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Single Gene ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

Abstract Etiolated maize radicles (inbred Oh43) subjected to a brief heat shock synthesize a family of small heat shock proteins (≃18 kD) that is composed of at least 12 members. We previously described the cDNA-derived sequence of three maize shsp mRNAs (cMHSP18-1, cMHSP18-3, and cMHSP18-9). In this report, we demonstrate that the mRNA transcribed in vitro from one of these cDNAs (cMHSP 18-9) is responsible for the synthesis of three members of the shsp family, and we suggest that cMHSP18-3 may be responsible for the synthesis of three additional members and cMHSP18-1 for the synthesis of two other members of this family. The fact that these genes do not contain introns, coupled with the observations reported herein, suggest that maize may have established another method of using a single gene to produce a number of different proteins.

scholarly journals Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins

Biochemistry ◽  
2009 ◽  
Vol 48 (18) ◽  
pp. 3828-3837 ◽  
Author(s):  
Hassane S. Mchaourab ◽  
Jared A. Godar ◽  
Phoebe L. Stewart
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Stability ◽  
Small Heat Shock Proteins ◽  
Chaperone Activity ◽  
Shock Proteins

scholarly journals Small heat shock proteins inhibit in vitro Aβ1-42 amyloidogenesis

FEBS Letters ◽  
1997 ◽  
Vol 416 (1) ◽  
pp. 117-121 ◽  
Author(s):  
Yogish C Kudva ◽  
Henry J Hiddinga ◽  
Peter C Butler ◽  
Cheryl S Mueske ◽  
Norman L Eberhardt
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals In Vitro Structural and Functional Characterization of the Small Heat Shock Proteins (sHSP) of the Cyanophage S-ShM2 and Its Host, Synechococcus sp. WH7803

PLoS ONE ◽  
2016 ◽  
Vol 11 (9) ◽  
pp. e0162233 ◽  
Author(s):  
Maxime Bourrelle-Langlois ◽  
Geneviève Morrow ◽  
Stéphanie Finet ◽  
Robert M. Tanguay
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Functional Characterization ◽  
Small Heat Shock Proteins ◽  
Synechococcus Sp ◽  
Shock Proteins

scholarly journals Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins

2000 ◽  
Vol 275 (47) ◽  
pp. 37212-37218 ◽  
Author(s):  
Sonja Studer ◽  
Franz Narberhaus
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Chaperone Activity ◽  
Oligomer Formation ◽  
Shock Proteins

Abstract 226: Human Cardiomyocytes Are Protected From Stress-induced Stiffening By Binding Of Small Heat Shock Proteins To Titin Spring Elements

2013 ◽  
Vol 113 (suppl_1) ◽  
Author(s):  
Sebastian Kotter ◽  
Andreas Unger ◽  
Nazha Hamdani ◽  
Wolfgang A Linke
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protective Effect ◽  
Small Heat Shock Proteins ◽  
Stress Conditions ◽  
Passive Stiffness ◽  
Human Cardiomyocytes ◽  
Αb Crystallin ◽  
Shock Proteins

Introduction: Small heat-shock proteins (sHSPs) generally participate in cellular protein quality-control mechanisms. They are abundant in cardiomyocytes where they bind under diverse stress conditions preferentially to myofilament proteins. The functional role of this association is unclear. Hypothesis: HSP27 and αB-crystallin bind to human cardiac titin spring elements and exert a protective effect on cardiomyocyte passive stiffness under stress conditions. Methods: Binding of sHSPs to recombinant human titin constructs was characterized by GST-pulldown assay and confirmed by immunofluorescence staining of human donor and failing (DCM) cardiomyocytes. Sedimentation-velocity centrifugation, photometric and chromatographic methods were used to test for titin aggregation and protection from it by sHSPs. Passive force was measured in isolated human cardiomyocytes or single myofibrils, in search for a possible protective effect of sHSPs on mechanical function. Results: HSP27 interacted with distinct domains of the human titin-spring region in vitro and in cardiomyocytes, and independent of the presence of actin filaments in the sarcomeres. The binding sites on the elastic titin segment resemble those for αB-crystallin and include proximal Ig-domains, the N2-B and N2-A regions, but not the PEVK-domain. In-vitro assays revealed a monomeric organization of these titin-spring elements; however, unfolded N2-A domain (mainly composed of Ig-domains) aggregated in pH-6.6 buffer but not in normal-pH buffer, whereas αB-crystallin protected from this effect. The intrinsically disordered N2-Bus titin domain did not aggregate. Single skinned human cardiomyocytes showed greatly increased passive stiffness when pre-stretched under acidic stress (pH 6.6), but αB-crystallin or HSP27 corrected the stiffening. In failing patient heart tissue, both HSP27 and αB-crystallin frequently associated with the elastic I-band region, in contrast to a cytosolic and Z-disk location of these sHSPs in donor heart. Conclusions: In cardiomyocytes sHSPs bind to mechanically active titin domains under stress conditions such as intracellular acidosis ( e.g. , ischemia), protecting the titin springs from aggregation and helping reverse diastolic stiffening.

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