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https://www.readbyqxmd.com/read/29442498/proteostasis-and-the-regulation-of-intra-and-extracellular-protein-aggregation-by-atp-independent-molecular-chaperones-lens-%C3%AE-crystallins-and-milk-caseins
#1
John A Carver, Heath Ecroyd, Roger J W Truscott, David C Thorn, Carl Holt
Molecular chaperone proteins perform a diversity of roles inside and outside the cell. One of the most important is the stabilization of misfolding proteins to prevent their aggregation, a process that is potentially detrimental to cell viability. Diseases such as Alzheimer's, Parkinson's, and cataract are characterized by the accumulation of protein aggregates. In vivo, many proteins are metastable and therefore under mild destabilizing conditions have an inherent tendency to misfold, aggregate, and hence lose functionality...
February 14, 2018: Accounts of Chemical Research
https://www.readbyqxmd.com/read/29397684/cardiovascular-small-heat-shock-protein-hspb7-is-a-kinetically-privileged-res-sensor
#2
Sanjna L Surya, Marcus J C Long, Daniel A Urul, Yi Zhao, Emily J Mercer, Islam M Elsaid, Todd Evans, Yimon Aye
Small heat shock protein (sHSP)-B7 (HSPB7) is a muscle-specific member of the non-ATP-dependent sHSPs. The precise role of HSPB7 is enigmatic. Here we disclose that zebrafish Hspb7 is a kinetically-privileged sensor able to react rapidly with native reactive electrophilic signals (RES), when only sub-stoichiometric amounts of RES are available in proximity to Hspb7 expressed in living cells. Among the two Hspb7-cysteines, this RES-sensing is fulfilled by a single cysteine (C117). Purification and characterizations in vitro reveal that the rate for RES-adduction is among the most efficient reported for protein-cysteines with native carbonyl-based-RES...
February 3, 2018: ACS Chemical Biology
https://www.readbyqxmd.com/read/29382725/the-small-heat-shock-protein-hsp27-binds-%C3%AE-synuclein-fibrils-preventing-elongation-and-cytotoxicity
#3
Dezerae Cox, Daniel R Whiten, James Brown, Mathew H Horrocks, Rebecca San Gil, Christopher M Dobson, David Klenerman, Antoine M van Oijen, Heath Ecroyd
Proteostasis, or protein homeostasis, encompasses the maintenance of the conformational and functional integrity of the proteome and involves an integrated network of cellular pathways. Molecular chaperones, such as the small heat shock proteins (sHsps), are a key element of the proteostasis network that have crucial roles in inhibiting the aggregation of misfolded proteins. Failure of the proteostasis network can lead to the accumulation of misfolded proteins into intra- and extracellular deposits. Deposits containing fibrillar forms of α- synuclein (α-syn) are characteristic of neurodegenerative disorders including Parkinson's disease and dementia with Lewy bodies...
January 30, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29190034/the-role-of-%C3%AE-b-crystallin-in-skeletal-and-cardiac-muscle-tissues
#4
REVIEW
Ivan Dimauro, Ambra Antonioni, Neri Mercatelli, Daniela Caporossi
All organisms and cells respond to various stress conditions such as environmental, metabolic, or pathophysiological stress by generally upregulating, among others, the expression and/or activation of a group of proteins called heat shock proteins (HSPs). Among the HSPs, special attention has been devoted to the mutations affecting the function of the αB-crystallin (HSPB5), a small heat shock protein (sHsp) playing a critical role in the modulation of several cellular processes related to survival and stress recovery, such as protein degradation, cytoskeletal stabilization, and apoptosis...
November 30, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/29177658/analysis-of-hspb1-hsp27-oligomerization-and-phosphorylation-patterns-and-its-interaction-with-specific-client-polypeptides
#5
André-Patrick Arrigo
Human HspB1 (also denoted as Hsp27) belongs to the family of small (or stress) proteins (sHsps). The family, which contains ten members including αA,B-crystallin polypeptides, is characterized by a conserved C-terminal α-crystallin domain and molecular weights ranging from 20 to 40 kDa. Here, procedures are described for analyzing the dynamic oligomerization and phosphorylation patterns of HspB1 in cells exposed to different environments. Changes in the structural organization of HspB1 can reprogram its interaction with specific partner/client polypeptides...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/29132139/study-of-hspb6-insights-into-the-properties-of-the-multifunctional-protective-agent
#6
Fazhao Li, Han Xiao, Fangfang Zhou, Zhiping Hu, Binbin Yang
HSPB6(Heat shock protein B6), is also referred to as P20/HSP20. Unlike other many other members of sHSP(small Heat shock protein) family, which tend to form high-molecular-mass oligomers, in solution, human HSPB6 only forms dimers. However, it still exhibits chaperon-like activity comparable with that of HSPB5. It is expressed ubiquitously, with high and constitutive expression in muscular tissues. sHSPs characteristically function as molecular chaperones and HSPB6 also has a molecular chaperone activity. HSPB6 is up-regulated in response to diverse cellular stress or damage and protect cells from otherwise lethal conditions...
November 13, 2017: Cellular Physiology and Biochemistry
https://www.readbyqxmd.com/read/29082555/chaperone-client-interactions-between-hsp21-and-client-proteins-monitored-in-solution-by-small-angle-x-ray-scattering-and-captured-by-crosslinking-mass-spectrometry
#7
Gudrun Rutsdottir, Morten Rasmussen, Peter Hojrup, Katja Bernfur, Cecilia Emanuelsson, Christopher A G Söderberg
The small heat shock protein (sHsp) chaperones are important for stress survival, yet the molecular details of how they interact with client proteins are not understood. All sHsps share a folded middle domain to which is appended flexible N- and C-terminal regions varying in length and sequence between different sHsps which, in different ways for different sHsps, mediate recognition of client proteins. In plants there is a chloroplast-localized sHsp, Hsp21, and a structural model suggests that Hsp21 has a dodecameric arrangement with six N-terminal arms located on the outside of the dodecamer and six inwardly-facing...
October 30, 2017: Proteins
https://www.readbyqxmd.com/read/29062969/rational-synthetic-combination-genetic-devices-boosting-high-temperature-ethanol-fermentation
#8
Huan Sun, Haiyang Jia, Jun Li, Xudong Feng, Yueqin Liu, Xiaohong Zhou, Chun Li
The growth and production of yeast in the industrial fermentation are seriously restrained by heat stress and exacerbated by heat induced oxidative stress. In this study, a novel synthetic biology approach was developed to globally boost the viability and production ability of S. cerevisiae at high temperature through rationally designing and combing heat shock protein (HSP) and superoxide dismutase (SOD) genetic devices to ultimately synergistically alleviate both heat stress and oxidative stress. HSP and SOD from extremophiles were constructed to be different genetic devices and they were preliminary screened by heat resistant experiments and anti-oxidative experiments, respectively...
June 2017: Synthetic and Systems Biotechnology
https://www.readbyqxmd.com/read/29062158/expression-of-cehsp17-protein-in-response-to-heat-shock-and-heavy-metal-ions
#9
Anastasia N Ezemaduka, Yunbiao Wang, Xiujun Li
Small heat shock proteins (sHSP) are ubiquitously found in all organisms, and with other heat shock proteins (HSP) such as HSP60, HSP70, HSP90, HSP100 made up the molecular chaperone family. They are involved in a wide range of biological processes which include among others cell resistance to biological and environmental stress conditions. In this study, we show by western blotting that CeHSP17, an sHSP of Caenorhabiditis elegans, is significantly induced by high temperatures. Furthermore, in response to metal stress, the CeHSP17 protein expression was significantly induced by cadmium and zinc at high concentration of clearly cytotoxic range in wild-type C...
September 2017: Journal of Nematology
https://www.readbyqxmd.com/read/29054823/characterization-and-expression-analysis-of-a-new-small-heat-shock-protein-hsp20-4-from-eimeria-tenella
#10
Hongyu Han, Yan Yan, Hui Dong, Shunhai Zhu, Qiping Zhao, Qi Zhai, Bing Huang
Small heat shock proteins (sHsps) are ubiquitous and diverse molecular chaperones. Found in almost all organisms, they regulate protein refolding and protect cells from stress. Until now, no sHsp has been characterized in Eimeria tenella. In this study, the novel EtsHsp20.4 gene was cloned from E. tenella by rapid amplification of cDNA ends based on a previously identified expressed sequence tag. The full-length cDNA was 1019bp in length and contained an open reading frame of 558bp that encoded a 185-amino acid polypeptide with a calculated molecular weight of 20...
October 18, 2017: Experimental Parasitology
https://www.readbyqxmd.com/read/29034430/ultraviolet-filters-and-heat-shock-proteins-effects-in-chironomus-riparius-by-benzophenone-3-and-4-methylbenzylidene-camphor
#11
Raquel Martín-Folgar, Mónica Aquilino, Irene Ozáez, José-Luis Martínez-Guitarte
Benzophenone-3 (BP3) and 4-methylbenzylidene camphor (4MBC) are common ultraviolet filters (UV filters), compounds considered as emergent contaminants, used in different products like plastics and personal care products. The levels of these compounds are rising in the wild, but the effects they have on invertebrates are poorly understood. Chironomus riparius is a benthic insect widely used in toxicology, and several studies have been previously performed in our laboratory to determine the effects these compounds have on this organism at the molecular level...
October 16, 2017: Environmental Science and Pollution Research International
https://www.readbyqxmd.com/read/28980406/characterization-and-functional-analysis-of-hsp18-3-gene-in-the-red-flour-beetle-tribolium-castaneum
#12
Jia Xie, Xing-Xing Hu, Meng-Fan Zhai, Xiao-Juan Yu, Xiao-Wen Song, Shan-Shan Gao, Wei Wu, Bin Li
Small heat shock proteins (sHSPs) are diverse and mainly function as molecular chaperones to protect organisms and cells from various stresses. In this study, hsp18.3, one Tribolium castaneum species-specific shsp, has been identified. Quantitative real-time PCR (qRT-PCR) illustrated that Tchsp18.3 is expressed in all developmental stages, and is highly expressed at early pupal and late adult stages. While, it highly expressed in ovary and fat body at adult period. Moreover, it was up-regulated 4532 ± 396-fold in response to enhanced heat stress but not to cold stress, meanwhile the lifespan of adults in ds-Tchsp18...
October 5, 2017: Insect Science
https://www.readbyqxmd.com/read/28832496/itraq-based-quantitative-proteomics-analysis-on-rice-anther-responding-to-high-temperature
#13
Qilin Mu, Wenying Zhang, Yunbo Zhang, Haoliang Yan, Ke Liu, Tsutomu Matsui, Xiaohai Tian, Pingfang Yang
As one of the most important crops, rice provides the major food for more than half of the world population. However, its production is limited by many environmental factors, among which high temperature stress (HS) frequently occurs during anthesis and reduces its spikelet fertility. To explore the mechanism of HS tolerance in rice, we conducted a comparative proteomics analysis on the anthers between HS resistant and sensitive cultivars under different levels of high temperature. Under the same HS treatment, the resistant cultivar showed much higher spikelet fertility than the sensitive cultivar...
August 23, 2017: International Journal of Molecular Sciences
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
#14
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
#15
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
#16
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
#17
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...
November 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
#18
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...
September 16, 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
#19
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
#20
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...
September 2017: Protein Science: a Publication of the Protein Society
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