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https://www.readbyqxmd.com/read/28332148/ph-dependent-structural-modulation-is-conserved-in-the-human-small-heat-shock-protein-hsbp1
#1
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
#2
Gudrun Rutsdottir, Johan Härmark, Yoran Weide, Hans Hebert, Morten Ib 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, of the cytosolic Hsp16.9. We took interest in Hsp21, a chloroplast-localized sHsp crucial for plant stress resistance, which has even longer N-terminals arms than Hsp16.9, with a functionally important and conserved methionine-rich motif...
March 21, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28320295/%C3%AE-crystallins-are-small-heat-shock-proteins-functional-and-structural-properties
#3
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
#4
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
#5
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
#6
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
#7
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
#8
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...
January 27, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28120291/role-of-shsps-in-organizing-cytosolic-protein-aggregation-and-disaggregation
#9
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...
January 24, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28074336/small-heat-shock-proteins-in-ageing-and-age-related-diseases
#10
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
https://www.readbyqxmd.com/read/28036392/a-differentiation-transcription-factor-establishes-muscle-specific-proteostasis-in-caenorhabditis-elegans
#11
Yael Bar-Lavan, Netta Shemesh, Shiran Dror, Rivka Ofir, Esti Yeger-Lotem, Anat Ben-Zvi
Safeguarding the proteome is central to the health of the cell. In multi-cellular organisms, the composition of the proteome, and by extension, protein-folding requirements, varies between cells. In agreement, chaperone network composition differs between tissues. Here, we ask how chaperone expression is regulated in a cell type-specific manner and whether cellular differentiation affects chaperone expression. Our bioinformatics analyses show that the myogenic transcription factor HLH-1 (MyoD) can bind to the promoters of chaperone genes expressed or required for the folding of muscle proteins...
December 2016: PLoS Genetics
https://www.readbyqxmd.com/read/27933463/effect-of-tempol-and-tempol-plus-catalase-on-intra-renal-haemodynamics-in-spontaneously-hypertensive-stroke-prone-shsp-and-wistar-rats
#12
Ahmad F Ahmeda, Mark G Rae, Mohammed F Al Otaibi, Lamyia M Anweigi, Edward J Johns
Vasoconstriction within the renal medulla contributes to the development of hypertension. This study investigated the role of reactive oxygen species (ROS) in regulating renal medullary and cortical blood perfusion (MBP and CBP respectively) in both stroke-prone spontaneously hypertensive rats (SHRSP) and Wistar rats. CBP and MBP were measured using a laser-Doppler flow meter before and after intra-renal infusion of tempol, the superoxide dismutase (SOD) mimetic or tempol plus catalase, the hydrogen peroxide-degrading enzyme...
December 9, 2016: Journal of Physiology and Biochemistry
https://www.readbyqxmd.com/read/27909051/the-chaperone-activity-and-substrate-spectrum-of-human-small-heat-shock-proteins
#13
Evgeny V Mymrikov, Marina Daake, Bettina Richter, Martin Haslbeck, Johannes Buchner
Small heat shock proteins (sHsps) are a ubiquitous family of molecular chaperones that suppress the unspecific aggregation of miscellaneous proteins. Multicellular organisms contain a large number of different sHsps, raising questions as to whether they function redundantly or are specialized in terms of substrates and mechanism. To gain insight into this issue, we undertook a comparative analysis of the eight major human sHsps on the aggregation of both model proteins and cytosolic lysates under standardized conditions...
January 13, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27901028/small-heat-shock-proteins-sequester-misfolding-proteins-in-near-native-conformation-for-cellular-protection-and-efficient-refolding
#14
Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P Mayer, Axel Mogk, Bernd Bukau
Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps, Hsp26 and Hsp42, we show in vitro that model substrates retain near-native state and are kept physically separated when complexed with either sHsp, while being completely unfolded when aggregated without sHsps...
November 30, 2016: Nature Communications
https://www.readbyqxmd.com/read/27889514/cadmium-alters-the-expression-of-small-heat-shock-protein-genes-in-the-aquatic-midge-chironomus-riparius
#15
Raquel Martín-Folgar, José-Luis Martínez-Guitarte
Cadmium (Cd) is a widespread and highly toxic heavy metal of particular ecotoxicological relevance for aquatic ecosystems. It occurs naturally in the environment but is also an industrial pollutant with extensively researched carcinogenic potentials. Heat shock proteins (HSPs) are chaperones that play an important role in maintaining protein homeostasis under stress conditions. Small heat shock proteins (sHSPs) comprise the most diverse group of the HSPs family. They are expressed both constitutively and by stress-induction...
February 2017: Chemosphere
https://www.readbyqxmd.com/read/27659778/effects-of-long-term-heat-stress-and-dietary-restriction-on-the-expression-of-genes-of-steroidogenic-pathway-and-small-heat-shock-proteins-in-rat-testicular-tissue
#16
F Bozkaya, M O Atli, A Guzeloglu, S A Kayis, M E Yildirim, E Kurar, R Yilmaz, N Aydilek
The aim was to investigate the effects of long-term heat stress and dietary restriction on the expression of certain genes involving in steroidogenic pathway and small heat-shock proteins (sHSPs) in rat testis. Sprague Dawley rats (n = 24) were equally divided into four groups. Group I and II were kept at an ambient temperature of 22°C, while Groups III and IV were reared at 38°C for 9 weeks. Feed was freely available for Group I and Group III, while Group II and Group IV were fed 60% of the diet consumed by their ad libitum counterparts...
September 23, 2016: Andrologia
https://www.readbyqxmd.com/read/27649598/the-expression-and-function-of-hsp30-like-small-heat-shock-protein-genes-in-amphibians-birds-fish-and-reptiles
#17
REVIEW
John J Heikkila
Small heat shock proteins (sHSPs) are a superfamily of molecular chaperones with important roles in protein homeostasis and other cellular functions. Amphibians, reptiles, fish and birds have a shsp gene called hsp30, which was also referred to as hspb11 or hsp25 in some fish and bird species. Hsp30 genes, which are not found in mammals, are transcribed in response to heat shock or other stresses by means of the heat shock factor that is activated in response to an accumulation of unfolded protein. Amino acid sequence analysis revealed that representative HSP30s from different classes of non-mammalian vertebrates were distinct from other sHSPs including HSPB1/HSP27...
January 2017: Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
https://www.readbyqxmd.com/read/27643500/in-vitro-structural-and-functional-characterization-of-the-small-heat-shock-proteins-shsp-of-the-cyanophage-s-shm2-and-its-host-synechococcus-sp-wh7803
#18
Maxime Bourrelle-Langlois, Geneviève Morrow, Stéphanie Finet, Robert M Tanguay
We previously reported the in silico characterization of Synechococcus sp. phage 18 kDa small heat shock protein (HspSP-ShM2). This small heat shock protein (sHSP) contains a highly conserved core alpha crystalline domain of 92 amino acids and relatively short N- and C-terminal arms, the later containing the classical C-terminal anchoring module motif (L-X-I/L/V). Here we establish the oligomeric profile of HspSP-ShM2 and its structural dynamics under in vitro experimental conditions using size exclusion chromatography (SEC/FPLC), gradient native gels electrophoresis and dynamic light scattering (DLS)...
2016: PloS One
https://www.readbyqxmd.com/read/27641668/differential-phosphorylation-based-regulation-of-%C3%AE-b-crystallin-chaperone-activity-for-multipass-transmembrane-proteins
#19
Michela Ciano, Simona Allocca, Maria Camilla Ciardulli, Lucrezia Della Volpe, Stefano Bonatti, Massimo D'Agostino
We have previously shown that αB-crystallin (CRYAB), a small heat shock protein (sHsp) that prevents irreversible aggregation of unfolded protein by an ATP-independent chaperone activity, plays a pivotal role in the biogenesis of multipass transmembrane proteins (TMPs) assisting their folding from the cytosolic side of the endoplasmic reticulum (ER) (D'Agostino et al., 2013). Here we present evidence, based on phosphomimetic substitutions, that the three phosphorytable serine residues at position 19, 45 and 59 of CRYAB play a different regulatory role in this novel chaperone activity: S19 and S45 have a strong inhibitory effect, either alone or in combination, while S59 has not and counteracts the inhibition caused by single phosphomimetic substitutions at S19 and S45...
October 14, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27639642/expression-and-promoter-analysis-of-the-oshsp16-9c-gene-in-rice
#20
Yan Zhang, Baohong Zou, Shan Lu, Yuan Ding, He Liu, Jian Hua
Small heat shock proteins (sHSPs) are molecular chaperones important for stress tolerance. In this study, heat induction of a rice sHSP gene OsHSP16.9C is analyzed to understand the molecular mechanisms underlying gene expression regulation in heat shock responses in rice. Promoter deletion analysis of the OsHSP16.9C using the luciferase (LUC) reporter gene in transgenic rice identifies a critical role of a promoter fragment containing an imperfect heat shock element (HSE) in heat induction. HSE was shown to be important for heat induction of AtHSP18...
October 14, 2016: Biochemical and Biophysical Research Communications
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