Hsp20

Last update 08 May 2025

Basic Info

Synonyms

FLJ32389, Heat shock 20 kDa-like protein p20, Heat shock protein beta-6

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Introduction

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.

100 Clinical Results associated with Hsp20

100 Translational Medicine associated with Hsp20

0 Patents (Medical) associated with Hsp20

618

Literatures (Medical) associated with Hsp20

01 May 2025·International Journal of Biological Macromolecules

Phylogenetic and expression analysis of HSP20 gene family in Rhododendron species of different altitudes

Article

Author: Liu, Meng-Xuan ; Zhang, Xiao-Mian ; Liu, Bing ; Xia, Yi-Ping ; Wang, Xiu-Yun ; Zhou, Hong ; Cao, Yu-Qing

Small heat shock proteins (sHSPs/HSP20s) play important roles in regulating plant growth, development and stress responses, especially heat stress. Rhododendron plants are major components in landscaping or potting, but poor high-temperature tolerance limits their wide application. To elucidate the adaptive differences between Rhododendron species inhabiting high- and low-altitude regions, this study identified a total of 265 HSP20 genes across seven Rhododendron species, with categorizing into 11 subfamilies. In the CI subfamily, low-altitude Rhododendron species had more HSP20 genes than high-altitude species. Ka/Ks analysis indicated that nearly all HSP20 genes in the seven Rhododendron species have undergone purifying selection, with only a few in the low-altitude species exhibiting positive selection. Analysis of cis-acting elements revealed that most HSP20 genes in R. ovatum and R. simsii could respond to a variety of plant hormones and stresses. Expression pattern analysis revealed that HSP20 members are implicated in flower development and response to heat stress, with the CI subfamily being the main branch responsible for the heat stress response in low-altitude Rhododendron species. Heat stress treatment of transgenic yeast further validated the crucial role of CI subfamily genes in heat stress tolerance. This study provides the first analysis of evolutionary differences in the HSP20 gene families between high- and low-altitude Rhododendron species. It offers insights into the evolutionary direction of HSP20 genes and identifies key genes related to heat tolerance. Additionally, it highlights the role of CI subfamily genes in heat stress tolerance, contributing to the development of heat-tolerant Rhododendron varieties and advancing flower development research.

01 May 2025·Biochimie

Interaction of small heat shock proteins with BAG3

Article

Author: Zabolotskii, Arthur I ; Zamotina, Maria A ; Muranova, Lydia K ; Gusev, Nikolai B

BAG3 is a universal adapter protein involved in various cellular processes, including the regulation of apoptosis, chaperone-assisted selective autophagy, and heat shock protein function. The interaction between small heat shock proteins (sHsps) and their α-crystallin domains (Acds) with full-length BAG3 protein and its IPV domain was analyzed using size-exclusion chromatography, native gel electrophoresis, and chemical cross-linking. HspB7 and the 3D mutant of HspB1 (which mimics phosphorylation) showed no interaction, HspB6 weakly interacted, and HspB8 strongly interacted with full-length BAG3. In contrast to the full-length sHsps, their α-crystallin domains (AcdB1, AcdB5, and AcdB6) were able to interact with BAG3, with AcdB8 again being the strongest interactor. Among all the full-length sHsps analyzed, only HspB8 bound to the IPV domain of BAG3. AcdB1, AcdB5, AcdB6, and AcdB8 interacted with the IPV domain of BAG3, with AcdB8 displaying the highest binding efficiency. The stoichiometry of crosslinked complexes formed by HspB8 (or its Acd) and the IPV domain of BAG3 was 2:1, whereas for the other sHsps and their Acds, it was 1:1. These findings suggest that while the IPV domain of BAG3 and the Acds of sHsps play an important role in binding, other structural regions significantly contribute to this interaction. The unique binding efficiency between BAG3 and HspB8 may be attributed to the intrinsic disorder and simple oligomeric structure of HspB8.

01 Apr 2025·World Journal of Microbiology and Biotechnology

Adaptive response of the holdase chaperone network of Acidithiobacillus ferrooxidans ATCC 23270 to stresses and energy sources

Article

Author: Mardonez, Mick Parra ; Izquierdo-Fiallo, Katherin ; Tello, Mario ; Rafaja, David ; Orellana, Omar ; Muñoz-Villagrán, Claudia ; Schlömann, Michael ; Levicán, Gloria ; Schimpf, Christian

Acidithiobacillus ferrooxidans is a chemolithoautotrophic acidophilic bacterium belonging to microbial communities involved in sulfide ore bioleaching. This microorganism possesses redundancy of genes encoding ATP-independent chaperone holdases like Hsp20 (hps20.1, hsp20.2, and hsp20.3), Hsp31, Hsp33, RidA (ridA.1 and ridA.2), and Lon (lon.1, lon.2, and lon.3), and single copy genes encoding SlyD and CnoX. We evaluated the response of these holdases to short and long-term stresses induced by changes in temperature (30° to 37 °C), pH (1.6 to 1.2 or 2.0), and oxidative status (1 mM H₂O₂) as well as to different energy sources (iron, sulfur, pyrite, sphalerite or chalcopyrite). Cells adapted under thermal and oxidative stress conditions showed a generalized upregulation of holdase genes, while short-term stress led to more discrete increases in transcript levels, with only hsp20.2 and hsp31 showing higher mRNA levels. hsp31 was also upregulated under acidic stresses, sulfur and sulfides. hsp20 variants showed different mRNA levels under different conditions, and cnoX was induced under oxidative conditions. Cells cultured on chalcopyrite had similar responses to those grown with peroxide. With some exceptions, stresses led to significant increases in intracellular ROS content, and decreases in ATP. These results pave the way to understanding proteostasis systems in extreme acidophilic bacteria.

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Hsp20

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