scholarly journals Quantitative Profiling of Arabidopsis Polar Glycerolipids under Two Types of Heat Stress

Plants ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 693 ◽  
Author(s):  
Feng Qin ◽  
Liang Lin ◽  
Yanxia Jia ◽  
Weiqi Li ◽  
Buzhu Yu
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Membrane Lipids ◽  
Heat Acclimation ◽  
Cellular Level ◽  
Minor Effect ◽  
Wild Type ◽  
A Minor ◽  
Shock Proteins ◽  
Polar Glycerolipids

At the cellular level, the remodelling of membrane lipids and production of heat shock proteins are the two main strategies whereby plants survive heat stress. Although many studies related to glycerolipids and HSPs under heat stress have been reported separately, detailed alterations of glycerolipids and the role of HSPs in the alterations of glycerolipids still need to be revealed. In this study, we profiled the glycerolipids of wild-type Arabidopsis and its HSP101-deficient mutant hot-1 under two types of heat stress. Our results demonstrated that the alterations of glycerolipids were very similar in wild-type Arabidopsis and hot-1 during heat stress. Although heat acclimation led to a slight decrease of glycerolipids, the decrease of glycerolipids in plants without heat acclimation is more severe under heat shock. The contents of 36:x monogalactosyl diacylglycerol (MGDG) were slightly increased, whereas that of 34:6 MGDG and 34:4 phosphatidylglycerol (PG) were severely decreased during moderate heat stress. Our findings suggested that heat acclimation could reduce the degradation of glycerolipids under heat shock. Synthesis of glycerolipids through the prokaryotic pathway was severely suppressed, whereas that through the eukaryotic pathway was slightly enhanced during moderate heat stress. In addition, HSP101 has a minor effect on the alterations of glycerolipids under heat stress.

Identification of heat stress-susceptible and -tolerant phenotypes in goats in semiarid tropics

2018 ◽  
Vol 58 (7) ◽  
pp. 1349 ◽  
Author(s):  
P. K. Rout ◽  
R. Kaushik ◽  
N. Ramachandran ◽  
S. K. Jindal
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Physiological Response ◽  
Cellular Level ◽  
Production Performance ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Shock Proteins ◽  
Neutral Conditions

The production performance of livestock is influenced by short-term variation in weather pattern. Goat adapts to varied ecological conditions and maintains productivity; however, wide variation has been observed among individual animals in response to environmental stimuli in a population. The objective of the present study was to identify the contrasting phenotypes on the basis of the physiological response in goats during heat stress. The study utilised 138 Jamunapari and 242 Barbari goats during peak heat-stress period and 82 Jamunapari and Barbari goats under thermo-neutral conditions. The physiological response of goats to different environmental conditions was evaluated by recording various parameters such as rectal temperature (RT), respiration rate (RR) and heart rate (HR). The temperature humidity index varied from 85.36 to 89.80 and from 65.32 to 73.12 during heat-stress and thermo-neutral assessments respectively. There was direct increase in HR and RR (>25%) due to heat stress in the animals, as compared with those in thermo-neutral conditions. On the basis of the distribution of RR and HR values across the breed in the population, the individuals having a RR of ≥50 and a HR of ≥130 are recognised as heat stress-susceptible phenotypes and those having a RR of ≤30 and a HR of ≤100 are recognised as heat stress-tolerant individuals. Different biomarkers were analysed in plasma, while heat-shock proteins and leptin were analysed in tissue extracts by ELISA. C-reactive protein and HSP90 concentrations were significantly (P < 0.05) different between heat stress-susceptible and heat stress-tolerant individuals. Heat-shock proteins HSP70, HSP 90, and C-reactive protein and triiodothyronine were reliable indicators of long-term heat stress. Identification of contrasting phenotypes in regard to heat stress is necessary so as to evaluate the expression pattern at a cellular level, as well as physiological and biochemical parameters.

scholarly journals CaHSP18.1a, a Small Heat Shock Protein from Pepper (Capsicum Annuum L.), Positively Responds to Heat, Drought, and Salt Tolerance

Horticulturae ◽  
2021 ◽  
Vol 7 (5) ◽  
pp. 117
Author(s):  
Yan-Li Liu ◽  
Shuai Liu ◽  
Jing-Jing Xiao ◽  
Guo-Xin Cheng ◽  
Haq Saeed ul ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Abiotic Stresses ◽  
Transgenic Arabidopsis ◽  
Small Heat Shock Protein ◽  
Wild Type ◽  
Drought And Salt Tolerance ◽  
Drought And Salt Stresses ◽  
Shock Proteins ◽  
Resistance To Heat

Pepper is a thermophilic crop, shallow-rooted plant that is often severely affected by abiotic stresses such as heat, salt, and drought. The growth and development of pepper is seriously affected by adverse stresses, resulting in decreases in the yield and quality of pepper crops. Small heat shock proteins (s HSPs) play a crucial role in protecting plant cells against various stresses. A previous study in our laboratory showed that the expression level of CaHSP18.1a was highly induced by heat stress, but the function and mechanism of CaHSP18.1a responding to abiotic stresses is not clear. In this study, we first analyzed the expression of CaHSP18.1a in the thermo-sensitive B6 line and thermo-tolerant R9 line and demonstrated that the transcription of CaHSP18.1a was strongly induced by heat stress, salt, and drought stress in both R9 and B6, and that the response is more intense and earlier in the R9 line. In the R9 line, the silencing of CaHSP18.1a decreased resistance to heat, drought, and salt stresses. The silencing of CaHSP18.1a resulted in significant increases in relative electrolyte leakage (REL) and malonaldehyde (MDA) contents, while total chlorophyll content decreased under heat, salt, and drought stresses. Overexpression analyses of CaHSP18.1a in transgenic Arabidopsis further confirmed that CaHSP18.1a functions positively in resistance to heat, drought, and salt stresses. The transgenic Arabidopsis had higherchlorophyll content and activities of superoxide dismutase, catalase, and ascorbate peroxidase than the wild type (WT). However, the relative conductivity and MDA content were decreased in transgenic Arabidopsis compared to the wild type (WT). We further showed that the CaHSP18.1a protein is localized to the cell membrane. These results indicate CaHSP18.1a may act as a positive regulator of responses to abiotic stresses.

scholarly journals Proteomic analysis of heat shock proteins in maize (Zea mays L.)

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Mahmoud Hussien Abou-Deif ◽  
Mohamed Abdel-Salam Rashed ◽  
Kamal Mohamed Khalil ◽  
Fatma El-Sayed Mahmoud
Keyword(s):  
Heat Treatment ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Proteome Analysis ◽  
High Temperature Stress ◽  
Heat Treatments ◽  
Maize Plants ◽  
Adverse Influence ◽  
Shock Proteins

Abstract Background Maize is one of the important cereal food crops in the world. High temperature stress causes adverse influence on plant growth. When plants are exposed to high temperatures, they produce heat shock proteins (HSPs), which may impart a generalized role in tolerance to heat stress. Proteome analysis was performed in plant to assess the changes in protein types and their expression levels under abiotic stress. The purpose of the study is to explore which proteins are involved in the response of the maize plant to heat shock treatment. Results We investigated the responses of abundant proteins of maize leaves, in an Egyptian inbred line of maize “K1”, upon heat stress through two-dimensional electrophoresis (2-DE) on samples of maize leaf proteome. 2-DE technique was used to recognize heat-responsive protein spots using Coomassie Brilliant Blue (CBB) and silver staining. In 2-D analysis of proteins from plants treated at 45 °C for 2 h, the results manifested 59 protein spots (4.3%) which were reproducibly detected as new spots where did not present in the control. In 2D for treated plants for 4 h, 104 protein spots (7.7%) were expressed only under heat stress. Quantification of spot intensities derived from heat treatment showed that twenty protein spots revealed clear differences between the control and the two heat treatments. Nine spots appeared with more intensity after heat treatments than the control, while four spots appeared only after heat treatments. Five spots were clearly induced after heat treatment either at 2 h or 4 h and were chosen for more analysis by LC-MSMS. They were identified as ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/Chaperonin. Conclusion The results revealed that the expressive level of the four heat shock proteins that were detected in this study plays important roles to avoid heat stress in maize plants.

Localization of metallothionein, heat shock protein (Hsp70), and superoxide dismutase expression in Hemidiaptomus roubaui (Copepoda, Crustacea) exposed to cadmium and heat stress

2007 ◽  
Vol 85 (3) ◽  
pp. 362-371 ◽  
Author(s):  
Martine Liberge ◽  
Roxane-M. Barthélémy
Keyword(s):  
Superoxide Dismutase ◽  
Heat Stress ◽  
Heat Shock ◽  
Metal Binding ◽  
Stress Proteins ◽  
Reproductive Function ◽  
Cadmium Stress ◽  
Specific Distribution ◽  
Freshwater Crustacean ◽  
Shock Proteins

Immunohistochemical methods were applied in the present study to investigate the expression of stress proteins such as metallothioneins (MT), which are metal-binding proteins, and heat shock proteins (Hsp70), as well as an antioxidant enzyme (superoxide dismutase, SOD), in the freshwater crustacean copepod Hemidiaptomus roubaui (Richard, 1888) exposed to cadmium or heat stress. The results show a tissue-specific distribution of MT-like protein after cadmium exposure in the brain and in the nerve cord. Cadmium stress did not provoke inducible Hsp70 or SOD expression. Unlike cadmium, heat stress induced the expression of Hsp70 and SOD in the shell glands, a structure involved in the reproductive function, and more particularly in the formation of the diapause egg envelope. MT expression is not induced in animals exposed to heat stress.

Herpes simplex virus type 2 UL14 gene product has heat shock protein(HSP)-like functions

2002 ◽  
Vol 115 (12) ◽  
pp. 2517-2527
Author(s):  
Yohei Yamauchi ◽  
Kaoru Wada ◽  
Fumi Goshima ◽  
Tohru Daikoku ◽  
Kenzo Ohtsuka ◽  
...  
Keyword(s):  
Heat Shock ◽  
Nuclear Translocation ◽  
Osmotic Shock ◽  
Minor Component ◽  
Firefly Luciferase ◽  
Hsp70 Family ◽  
Arginine Residues ◽  
Simplex Virus ◽  
A Minor ◽  
Shock Proteins

The HSV-2 UL14 gene encodes a 32 kDa protein that is a minor component of the viral tegument. The protein relocates other viral proteins such as VP26 and UL33 protein into the nuclei of transiently coexpressing cells(Yamauchi et al., 2001). We found that the protein shared some characteristics of heat shock proteins(HSPs) or molecular chaperones, such as nuclear translocation upon heat shock,ATP deprivation and osmotic shock. Interestingly, a significant homology over a stretch of 15 amino acids was found between an N-terminal region of HSV UL14 protein and the substrate-binding domain of Hsp70 family proteins. Two arginine residues in this region were important for nuclear translocation of VP26. In addition, overexpression of UL14 protein increased the activity of coexpressed firefly luciferase, which suggested that the protein functioned in the folding of newly synthesized luciferase. We thus conclude that UL14 protein can act as a chaperone-like protein in a singly expressed state.

scholarly journals Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

2018 ◽  
Vol 50 (5) ◽  
pp. 1617-1637 ◽  
Author(s):  
Gang-Zheng Wang ◽  
Chao-Jun Ma ◽  
Yi Luo ◽  
Sha-Sha Zhou ◽  
Yan Zhou ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Indoleacetic Acid ◽  
Lentinula Edodes ◽  
Acid Biosynthesis ◽  
Over Expression ◽  
Indoleacetic Acid Biosynthesis ◽  
Shock Proteins ◽  
Exogenous Iaa

Background/Aims: Heat stress could cause huge losses for Lentinula edodes in China and other Asian cultivation areas. Yet our understanding of mechanism how to defend to heat stress is incomplete. Methods: Using heat-tolerant and heat-sensitive strains of L. edodes, we reported a combined proteome and transcriptome analysis of L. edodes response to 40 °C heat stress for 24 h. Meanwhile, the effect of LeDnaJ on the thermotolerance and IAA (indoleacetic acid) biosynthesis in L. edodes was analyzed via the over-expression method. Results: The proteome results revealed that HSPs (heat shock proteins) such as Hsp40 (DnaJ), Hsp70, Hsp90 and key enzymes involved in tryptophan and IAA metabolism process LeTrpE, LeTrpD, LeTam-1, LeYUCCA were more highly expressed in S606 than in YS3357, demonstrating that HSPs and tryptophan as well as IAA metabolism pathway should play an important role in thermotolerance. Over-expression of LeDnaJ gene in S606 strains showed better tolerance to heat stress. It was also documented that intracellular IAA accumulation of S606 (8-fold up) was more than YS3357 (2-fold up), and exogenous IAA enhanced L. edodes tolerance to heat stress. Conclusion: Our data support the interest of LeTrpE, LeDnaJ, tryptophan and IAA could play a pivotal role in enhancing organism thermotolerance.

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