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https://www.readbyqxmd.com/read/28608391/the-chloroplast-localized-small-heat-shock-protein-hsp21-associates-with-the-thylakoid-membranes-in-heat-stressed-plants
#1
Katja Bernfur, Gudrun Rutsdottir, Cecilia Emanuelsson
The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps, with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues...
June 12, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28566710/massive-expansion-and-differential-evolution-of-small-heat-shock-proteins-with-wheat-triticum-aestivum-l-polyploidization
#2
Xiaoming Wang, Ruochen Wang, Chuang Ma, Xue Shi, Zhenshan Liu, Zhonghua Wang, Qixin Sun, Jun Cao, Shengbao Xu
Wheat (Triticum aestivum), one of the world's most important crops, is facing unprecedented challenges due to global warming. To evaluate the gene resources for heat adaptation in hexaploid wheat, small heat shock proteins (sHSPs), the key plant heat protection genes, were comprehensively analysed in wheat and related species. We found that the sHSPs of hexaploid wheat were massively expanded in A and B subgenomes with intrachromosomal duplications during polyploidization. These expanded sHSPs were under similar purifying selection and kept the expressional patterns with the original copies...
May 31, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28547731/proline-isomerization-in-the-c-terminal-region-of-hsp27
#3
T Reid Alderson, Justin L P Benesch, Andrew J Baldwin
In mammals, small heat-shock proteins (sHSPs) typically assemble into interconverting, polydisperse oligomers. The dynamic exchange of sHSP oligomers is regulated, at least in part, by molecular interactions between the α-crystallin domain and the C-terminal region (CTR). Here we report solution-state nuclear magnetic resonance (NMR) spectroscopy investigations of the conformation and dynamics of the disordered and flexible CTR of human HSP27, a systemically expressed sHSP. We observed multiple NMR signals for residues in the vicinity of proline 194, and we determined that, while all observed forms are highly disordered, the extra resonances arise from cis-trans peptidyl-prolyl isomerization about the G193-P194 peptide bond...
July 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28520783/effect-of-n-terminal-region-of-nuclear-drosophila-melanogaster-small-heat-shock-protein-dmhsp27-on-function-and-quaternary-structure
#4
Mohamed Taha Moutaoufik, Geneviève Morrow, Stéphanie Finet, Robert M Tanguay
The importance of the N-terminal region (NTR) in the oligomerization and chaperone-like activity of the Drosophila melanogaster small nuclear heat shock protein DmHsp27 was investigated by mutagenesis using size exclusion chromatography and native gel electrophoresis. Mutation of two sites of phosphorylation in the N-terminal region, S58 and S75, did not affect the oligomerization equilibrium or the intracellular localization of DmHsp27 when transfected into mammalian cells. Deletion or mutation of specific residues within the NTR region delineated a motif (FGFG) important for the oligomeric structure and chaperone-like activity of this sHsp...
2017: PloS One
https://www.readbyqxmd.com/read/28487364/specific-sequences-in-the-n-terminal-domain-of-human-small-heat-shock-protein-hspb6-dictate-preferential-hetero-oligomerization-with-the-orthologue-hspb1
#5
Michelle Heirbaut, Frederik Lermyte, Esther M Martin, Steven Beelen, Frank Sobott, Sergei V Strelkov, Stephen D Weeks
Small heat-shock proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular proteostasis. Although sHSPs are characterized by their small monomeric weight, they typically assemble into large polydisperse oligomers that vary in both size and shape but are principally composed of dimeric building blocks. These assemblies can include different sHSP orthologues, creating additional complexity that may affect chaperone activity. However, the structural and functional properties of such hetero-oligomers are poorly understood...
June 16, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28462052/cloning-and-evaluation-of-reference-genes-for-quantitative-real-time-pcr-analysis-in-amorphophallus
#6
Kai Wang, Yi Niu, Qijun Wang, Haili Liu, Yi Jin, Shenglin Zhang
Quantitative real-time reverse transcription PCR (RT-qPCR) has been widely used in the detection and quantification of gene expression levels because of its high accuracy, sensitivity, and reproducibility as well as its large dynamic range. However, the reliability and accuracy of RT-qPCR depends on accurate transcript normalization using stably expressed reference genes. Amorphophallus is a perennial plant with a high content of konjac glucomannan (KGM) in its corm. This crop has been used as a food source and as a traditional medicine for thousands of years...
2017: PeerJ
https://www.readbyqxmd.com/read/28455764/heterologous-expression-of-three-camellia-sinensis-small-heat-shock-protein-genes-confers-temperature-stress-tolerance-in-yeast-and-arabidopsis-thaliana
#7
Mingle Wang, Zhongwei Zou, Qinghui Li, Huahong Xin, Xujun Zhu, Xuan Chen, Xinghui Li
CsHSP17.7, CsHSP18.1, and CsHSP21.8 expressions are induced by heat and cold stresses, and CsHSP overexpression confers tolerance to heat and cold stresses in transgenic Pichia pastoris and Arabidopsis thaliana. Small heat shock proteins (sHSPs) are crucial for protecting plants against biotic and abiotic stresses, especially heat stress. However, knowledge concerning the functions of Camellia sinensis sHSP in heat and cold stresses remains poorly understood. In this study, three C. sinensis sHSP genes (i.e...
July 2017: Plant Cell Reports
https://www.readbyqxmd.com/read/28450727/the-cshsp17-2-molecular-chaperone-is-essential-for-thermotolerance-in-camellia-sinensis
#8
Mingle Wang, Zhongwei Zou, Qinghui Li, Kang Sun, Xuan Chen, Xinghui Li
Small heat shock proteins (sHSPs) play important roles in responses to heat stress. However, the functions of sHSPs in tea plants (Camellia sinensis) remain uncharacterized. A novel sHSP gene, designated CsHSP17.2, was isolated from tea plants. Subcellular localization analyses indicated that the CsHSP17.2 protein was present in the cytosol and the nucleus. CsHSP17.2 expression was significantly up-regulated by heat stress but was unaffected by low temperature. The CsHSP17.2 transcript levels increased following salt and polyethylene glycol 6000 treatments but decreased in the presence of abscisic acid...
April 27, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28364346/the-growing-world-of-small-heat-shock-proteins-from-structure-to-functions
#9
REVIEW
Serena Carra, Simon Alberti, Patrick A Arrigo, Justin L Benesch, Ivor J Benjamin, Wilbert Boelens, Britta Bartelt-Kirbach, Bianca J J M Brundel, Johannes Buchner, Bernd Bukau, John A Carver, Heath Ecroyd, Cecilia Emanuelsson, Stephanie Finet, Nikola Golenhofen, Pierre Goloubinoff, Nikolai Gusev, Martin Haslbeck, Lawrence E Hightower, Harm H Kampinga, Rachel E Klevit, Krzysztof Liberek, Hassane S Mchaourab, Kathryn A McMenimen, Angelo Poletti, Roy Quinlan, Sergei V Strelkov, Melinda E Toth, Elizabeth Vierling, Robert M Tanguay
Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental roles in cell biology. sHSPs are key components of the cellular protein quality control system, acting as the first line of defense against conditions that affect protein homeostasis and proteome stability, from bacteria to plants to humans. sHSPs have the ability to bind to a large subset of substrates and to maintain them in a state competent for refolding or clearance with the assistance of the HSP70 machinery. sHSPs participate in a number of biological processes, from the cell cycle, to cell differentiation, from adaptation to stressful conditions, to apoptosis, and, even, to the transformation of a cell into a malignant state...
July 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28337642/the-small-heat-shock-proteins-%C3%AE-b-crystallin-hspb5-and-hsp27-hspb1-inhibit-the-intracellular-aggregation-of-%C3%AE-synuclein
#10
Dezerae Cox, Heath Ecroyd
Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. Proteostasis is preserved in the face of stress by a complex network of cellular machinery, including the small heat shock molecular chaperone proteins (sHsps), which act to inhibit the aggregation and deposition of misfolded protein intermediates. Despite this, the pathogenesis of several neurodegenerative diseases has been inextricably linked with the amyloid fibrillar aggregation and deposition of α-synuclein (α-syn)...
July 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28332148/ph-dependent-structural-modulation-is-conserved-in-the-human-small-heat-shock-protein-hsbp1
#11
Amanda F Clouser, Rachel E Klevit
The holdase activity and oligomeric propensity of human small heat shock proteins (sHSPs) are regulated by environmental factors. However, atomic-level details are lacking for the mechanisms by which stressors alter sHSP responses. We previously demonstrated that regulation of HSPB5 is mediated by a single conserved histidine over a physiologically relevant pH range of 6.5-7.5. Here, we demonstrate that HSPB1 responds to pH via a similar mechanism through pH-dependent structural changes that are induced via protonation of the structurally analogous histidine...
March 22, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28325834/structural-model-of-dodecameric-heat-shock-protein-hsp21-flexible-n-terminal-arms-interact-with-client-proteins-while-c-terminal-tails-maintain-the-dodecamer-and-chaperone-activity
#12
Gudrun Rutsdottir, Johan Härmark, Yoran Weide, Hans Hebert, Morten I Rasmussen, Sven Wernersson, Michal Respondek, Mikael Akke, Peter Højrup, Philip J B Koeck, Christopher A G Söderberg, Cecilia Emanuelsson
Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural information; currently, there is only one high-resolution structure of a plant sHsp published, that of the cytosolic Hsp16.9. We took interest in Hsp21, a chloroplast-localized sHsp crucial for plant stress resistance, which has even longer N-terminal arms than Hsp16.9, with a functionally important and conserved methionine-rich motif...
May 12, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28320295/%C3%AE-crystallins-are-small-heat-shock-proteins-functional-and-structural-properties
#13
REVIEW
T S Tikhomirova, O M Selivanova, O V Galzitskaya
During its life cycle, a cell can be subjected to various external negative effects. Many proteins provide cell protection, including small heat shock proteins (sHsp) that have chaperone-like activity. These proteins have several important functions involving prevention of apoptosis and retention of cytoskeletal integrity; also, sHsp take part in the recovery of enzyme activity. The action mechanism of sHsp is based on the binding of hydrophobic regions exposed to the surface of a molten globule. α-Crystallins presented in chordate cells as two αA- and αB-isoforms are the most studied small heat shock proteins...
February 2017: Biochemistry. Biokhimii︠a︡
https://www.readbyqxmd.com/read/28248227/calcium-homeostasis-and-muscle-energy-metabolism-are-modified-in-hspb1-null-mice
#14
Brigitte Picard, Malek Kammoun, Mohammed Gagaoua, Christiane Barboiron, Bruno Meunier, Christophe Chambon, Isabelle Cassar-Malek
Hsp27-encoded by HspB1-is a member of the small heat shock proteins (sHsp, 12-43 kDa (kilodalton)) family. This protein is constitutively present in a wide variety of tissues and in many cell lines. The abundance of Hsp27 is highest in skeletal muscle, indicating a crucial role for muscle physiology. The protein identified as a beef tenderness biomarker was found at a crucial hub in a functional network involved in beef tenderness. The aim of this study was to analyze the proteins impacted by the targeted invalidation of HspB1 in the Tibialis anterior muscle of the mouse...
May 4, 2016: Proteomes
https://www.readbyqxmd.com/read/28219929/hsp70-displaces-small-heat-shock-proteins-from-aggregates-to-initiate-protein-refolding
#15
Szymon Żwirowski, Agnieszka Kłosowska, Igor Obuchowski, Nadinath B Nillegoda, Artur Piróg, Szymon Ziętkiewicz, Bernd Bukau, Axel Mogk, Krzysztof Liberek
Small heat shock proteins (sHsps) are an evolutionary conserved class of ATP-independent chaperones that protect cells against proteotoxic stress. sHsps form assemblies with aggregation-prone misfolded proteins, which facilitates subsequent substrate solubilization and refolding by ATP-dependent Hsp70 and Hsp100 chaperones. Substrate solubilization requires disruption of sHsp association with trapped misfolded proteins. Here, we unravel a specific interplay between Hsp70 and sHsps at the initial step of the solubilization process...
March 15, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28219754/identification-of-responsive-proteins-in-panonychus-citri-exposed-to-abamectin-by-a-proteomic-approach
#16
Xiao-Min Shen, Rui Zhong, Wen-Kai Xia, Dong Wei, Tian-Bo Ding, Chong-Yu Liao, Jin-Zhi Niu, Wei Dou, Jin-Jun Wang
Abamectin is a microbial-derived pesticide widely used for control of agricultural pests. However, sustained use of abamectin has led to the development of resistance in some target species. Previous studies on arthropod resistance to abamectin have mainly used traditional biochemical and molecular approaches. To understand the responses of citrus red mite, Panonychus citri, exposed to abamectin, comparative proteomic analysis was conducted using two-dimensional electrophoresis (2-DE). A total of 26 distinct protein spots were present in response to abamectin exposure...
February 20, 2017: Journal of Proteomics
https://www.readbyqxmd.com/read/28178571/genome-wide-identification-and-analysis-of-biotic-and-abiotic-stress-regulation-of-small-heat-shock-protein-hsp20-family-genes-in-bread-wheat
#17
Senthilkumar K Muthusamy, Monika Dalal, Viswanathan Chinnusamy, Kailash C Bansal
Small Heat Shock Proteins (sHSPs)/HSP20 are molecular chaperones that protect plants by preventing protein aggregation during abiotic stress conditions, especially heat stress. Due to global climate change, high temperature is emerging as a major threat to wheat productivity. Thus, the identification of HSP20 and analysis of HSP transcriptional regulation under different abiotic stresses in wheat would help in understanding the role of these proteins in abiotic stress tolerance. We used sequences of known rice and Arabidopsis HSP20 HMM profiles as queries against publicly available wheat genome and wheat full length cDNA databases (TriFLDB) to identify the respective orthologues from wheat...
April 2017: Journal of Plant Physiology
https://www.readbyqxmd.com/read/28130664/chaperone-activity-of-human-small-heat-shock-protein-gst-fusion-proteins
#18
Hannah Arbach, Caley Butler, Kathryn A McMenimen
Small heat shock proteins (sHsps) are a ubiquitous part of the machinery that maintains cellular protein homeostasis by acting as molecular chaperones. sHsps bind to and prevent the aggregation of partially folded substrate proteins in an ATP-independent manner. sHsps are dynamic, forming an ensemble of structures from dimers to large oligomers through concentration-dependent equilibrium dissociation. Based on structural studies and mutagenesis experiments, it is proposed that the dimer is the smallest active chaperone unit, while larger oligomers may act as storage depots for sHsps or play additional roles in chaperone function...
July 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28120291/role-of-shsps-in-organizing-cytosolic-protein-aggregation-and-disaggregation
#19
REVIEW
Axel Mogk, Bernd Bukau
Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state...
July 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28074336/small-heat-shock-proteins-in-ageing-and-age-related-diseases
#20
REVIEW
Nikolaos Charmpilas, Emmanouil Kyriakakis, Nektarios Tavernarakis
Small heat shock proteins (sHSPs) are gatekeepers of cellular homeostasis across species, preserving proteome integrity under stressful conditions. Nonetheless, recent evidence suggests that sHSPs are more than molecular chaperones with merely auxiliary role. In contrast, sHSPs have emerged as central lifespan determinants, and their malfunction has been associated with the manifestation of neurological disorders, cardiovascular disease and cancer malignancies. In this review, we focus on the role of sHSPs in ageing and age-associated diseases and highlight the most prominent paradigms, where impairment of sHSP function has been implicated in human pathology...
January 10, 2017: Cell Stress & Chaperones
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