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https://www.readbyqxmd.com/read/28812232/introgression-of-heat-shock-protein-hsp70-and-shsp-genes-into-the-malaysian-elite-chilli-variety-kulai-capsicum-annuum-l-through-the-application-of-marker-assisted-backcrossing-mab
#1
Magaji G Usman, Mohd Y Rafii, Mohammad Y Martini, Oladosu A Yusuff, Mohd R Ismail, Gous Miah
Backcrossing together with simple sequence repeat marker strategy was adopted to improve popular Malaysian chilli Kulai (Capsicum annuum L.) for heat tolerance. The use of molecular markers in backcross breeding and selection contributes significantly to overcoming the main drawbacks such as increase linkage drag and time consumption, in the ancient manual breeding approach (conventional), and speeds up the genome recovery of the recurrent parent. The strategy was adopted to introgress heat shock protein gene(s) from AVPP0702 (C...
August 15, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28755305/identification-and-expression-analysis-of-multiple-small-heat-shock-protein-genes-in-spruce-budworm-choristoneura-fumiferana-l
#2
Guoxing Quan, Jun Duan, Tim Ladd, Peter J Krell
Fifteen small heat shock protein (sHSP) genes were identified from spruce budworm, Choristoneura fumiferana (L.), an important native forest pest in North America. The transcript levels of each CfHSP were measured under non-stress conditions in all life stages from egg to adult and in five different larval tissues. CfHSP transcript levels showed variation during development, with highest levels in adults and lowest in eggs. Most CfHSP transcripts are highly expressed in larval fat body and Malpighian tubules; two CfHSPs display extremely high expression in the head and epidermis...
July 28, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28743906/transient-regulation-of-three-clustered-tomato-class-i-small-heat-shock-chaperone-genes-by-ethylene-is-mediated-by-slmads-rin-transcription-factor
#3
Vijaya Shukla, Rakesh K Upadhyay, Mark L Tucker, James J Giovannoni, Sairam V Rudrabhatla, Autar K Mattoo
Clustered class-I small heat-shock protein (sHSP) chaperone genes, SlHSP17.6, SlHSP20.0 and SlHSP20.1, in tomato are demonstrated to be transcriptionally regulated by ethylene during mature green (MG) fruit transition into ripening. These genes are constitutively expressed at MG fruit stage in two different tomato genotypes as well as in their ripening mutants, including rin, nor and Nr, and an ethylene-deficient transgenic line, ACS2-antisense. Notably, ethylene treatment of the MG fruit led to significant sHSP gene suppression in both wild-types, ACS2-antisense, nor/nor and Nr/Nr, but not the rin/rin mutant...
July 25, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28735974/characteristics-of-six-small-heat-shock-protein-genes-from-bactrocera-dorsalis-diverse-expression-under-conditions-of-thermal-stress-and-normal-growth
#4
Wei Dou, Yi Tian, Hong Liu, Yan Shi, Guy Smagghe, Jin-Jun Wang
To explore the functions of small heat shock proteins (sHsps) in relation to thermal stress and development in Bactrocera dorsalis (Hendel), one of the most economically important pest species attacking a wide range of fruits and vegetables, six full-length cDNAs of sHsp genes (BdHsp17.7, 18.4, 20.4, 20.6, 21.6 and 23.8) were cloned, and the expression patterns in different developmental stages and tissues, as well as in response to both thermal and 20-hydroxyecdysone (20E) exposures, were examined using real time quantitative PCR...
July 21, 2017: Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
https://www.readbyqxmd.com/read/28720498/rna-aptamers-targeted-for-human-%C3%AE-a-crystallin-do-not-bind-%C3%AE-b-crystallin-and-spare-the-%C3%AE-crystallin-domain
#5
Prabhat K Mallik, Hua Shi, Jayanti Pande
The molecular chaperones, α-crystallins, belong to the small heat shock protein (sHSP) family and prevent the aggregation and insolubilization of client proteins. Studies in vivo have shown that the chaperone activity of the α-crystallins is raised or lowered in various disease states. Therefore, the development of tools to control chaperone activity may provide avenues for therapeutic intervention, as well as enable a molecular understanding of chaperone function. The major human lens α-crystallins, αA- (HAA) and αB- (HAB), share 57% sequence identity and show similar activity towards some clients, but differing activities towards others...
July 15, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28714602/genome-wide%C3%A2-identification-and-characterization%C3%A2-of%C3%A2-hsp-gene-superfamily-in-whitefly-bemisia-tabaci-and-expression-profiling%C3%A2-analysis%C3%A2-under-temperature-stress
#6
Xin-Ru Wang, Chao Wang, Fei-Xue Ban, Dan-Tong Zhu, Shu-Sheng Liu, Xiao-Wei Wang
Heat shock proteins (Hsp) are essential molecular chaperones that play important roles in the stress stimulation of insects. Bemisia tabaci, a phloem feeder and invasive species, can cause extensive crop damage through direct feeding and transmission of plant viruses. Here we employed comprehensive genomics approaches to identity HSP superfamily members in Middle East Asia Minor 1 whitefly genome. In total, we identified 26 Hsp genes, including 3 Hsp90, 17 Hsp70, 1 Hsp60 and 5 sHSP (small heat shock protein, sHSP) genes...
July 17, 2017: Insect Science
https://www.readbyqxmd.com/read/28608391/the-chloroplast-localized-small-heat-shock-protein-hsp21-associates-with-the-thylakoid-membranes-in-heat-stressed-plants
#7
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 of 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
#8
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
#9
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
#10
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
#11
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
#12
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
#13
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
#14
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
#15
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
#16
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
#17
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...
July 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
#18
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
#19
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
#20
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
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