Induction of Heat Shock Protein Genes is the Hallmark of Egg Heat Tolerance in Agasicles hygrophila (Coleoptera: Chrysomelidae)

2020 ◽  
Vol 113 (4) ◽  
pp. 1972-1981
Author(s):  
Dong Jia ◽  
Yan-Hong Liu ◽  
Bin Zhang ◽  
Zhou-Yu Ji ◽  
Yuan-Xin Wang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
High Temperatures ◽  
Heat Tolerance ◽  
Invasive Plant ◽  
Alternanthera Philoxeroides ◽  
Alligator Weed ◽  
Natural Habitats ◽  
Hsp Genes

Abstract Insects are ecotothermic organisms. Their development, survival, reproduction as well as distribution and abundance are affected by temperature. Heat shock protein (HSP) gene expression is closely associated with temperature variation and influences the adaptation of organisms to adverse environments. The beetle Agasicles hygrophila has successfully been used for biological control of the invasive plant alligator weed (Alternanthera philoxeroides). As A. hygrophila populations are substantially inhibited by high temperatures in the summer, increasing global temperatures may limit the efficacy of this control agent. We previously established that A. hygrophila eggs have low tolerance to heat and this factored into the decreased numbers of A. hygrophila beetles at temperatures of 37.5°C and above. Here, we identified 26 HSP genes in A. hygrophila and examined the relationship between the transcript levels of these genes and heat tolerance. The temperature at which the expression of these 21 HSP genes peaked (Tpeak) was 37.5°C, which is in line with the limit of the high temperatures that A. hygrophila eggs tolerate. Therefore, we speculate that the Tpeak of HSP gene expression in eggs indicates the upper limit of temperatures that A. hygrophila eggs tolerate. This study identifies HSP genes as potential robust biomarkers and emphasizes that determining species’ heat tolerance in their natural habitats remains an important consideration for biocontrol. HSP gene expression data provide information about a species’ heat tolerance and may be used to predict its geographical distribution.

scholarly journals Expression of heat shock protein (HSP) genes and antioxidant enzyme genes in hybrid rice II YOU 838 during heat stress

2021 ◽  
pp. 38-43
Author(s):  
Yan Wang ◽  
Min Huang ◽  
Peng Gao ◽  
Hao Chen ◽  
Yu Zheng ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heat Stress ◽  
High Temperature ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Antioxidant Enzyme ◽  
Heat Tolerance ◽  
Hybrid Rice ◽  
High Temperature Stress ◽  
Flag Leaves

II YOU 838 (Oryza sativa subsp. indica), crossed by the maternal II-32A and paternal Fu Hui 838, was one of the most widely cultivated hybrid rice in China. Fu Hui 838, which has resistance to high temperature, was generated by mutation technology in 1990. Previous field-testing showed that II YOU 838 had tolerance to high temperature stress and this was confirmed in the present study. The mechanism of heat tolerance of II YOU 838 is not understood. The present study reports gene expression of a representative sample of heat-responsive proteins in II YOU 838 flag leaves subjected to heat stress during flowering. Differential expression of the heat shock protein 70 (HSP70), heat shock protein 90 (HSP90), small heat shock protein (smHSP), superoxide dismutase (SOD), catalase (CAT) and peroxidase (POD) were studied under heat stress and optimum temperatures in flag leaves of II YOU 838. All six genes studied were responsive to high temperatures. Quantitative real-time PCR showed increased expression of the heat shock protein genes and antioxidant enzyme genes in flag leaves under heat stress. With increasing number of days gene expression decreased under high temperature. Peak expression of SOD, POD, hsp70 and hsp90 was on Day 2 under 39 ℃. On Day 3, the expression of CAT under 39 ℃ was the highest. The expression of smhsp was highest on Day 3 under 27 ℃, followed by that on Day 2 under 27 ℃. The maximum expression values were observed on Day 2 or Day 3 after beginning of heat stress. This suggests that hsp90, hsp70, SOD and POD are principally involved in early responses to heat in rice flag leaves, and that smhsp may play a role in the recovery mechanism in rice after heat stress. This may provide insights into the mechanism of heat-tolerance in rice

scholarly journals Heat Shock Protein 70 Improves In Vitro Embryo Yield and Quality from Heat Stressed Bovine Oocytes

Animals ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 1794
Author(s):  
Konstantina Stamperna ◽  
Themistoklis Giannoulis ◽  
Eleni Dovolou ◽  
Maria Kalemkeridou ◽  
Ioannis Nanas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Cumulus Cells ◽  
Intramolecular Interactions ◽  
Developmental Competence ◽  
Embryo Yield ◽  
Bovine Oocytes

Heat shock protein 70 (HSP70) is a chaperon that stabilizes unfolded or partially folded proteins, preventing inappropriate inter- and intramolecular interactions. Here, we examined the developmental competence of in vitro matured oocytes exposed to heat stress with or without HSP70. Bovine oocytes were matured for 24 h at 39 °C without (group C39) or with HSP70 (group H39) and at 41 °C for the first 6 h, followed by 16 h at 39 °C with (group H41) or without HSP70 (group C41). After insemination, zygotes were cultured for 9 days at 39 °C. Cleavage and embryo yield were assessed 48 h post insemination and on days 7, 8, 9, respectively. Gene expression was assessed by RT-PCR in oocytes, cumulus cells and blastocysts. In C41, blastocysts formation rate was lower than in C39 and on day 9 it was lower than in H41. In oocytes, HSP70 enhanced the expression of three HSP genes regardless of incubation temperature. HSP70 at 39 °C led to tight coordination of gene expression in oocytes and blastocysts, but not in cumulus cells. Our results imply that HSP70, by preventing apoptosis, supporting signal transduction, and increasing antioxidant protection of the embryo, protects heat stressed maturing bovine oocyte and restores its developmental competence.

Over-expression of a small heat shock protein, sHSP17.7, confers both heat tolerance and UV-B resistance to rice plants

2004 ◽  
Vol 13 (2) ◽  
pp. 165-175 ◽  
Author(s):  
Toyotaka Murakami ◽  
Shuichi Matsuba ◽  
Hideyuki Funatsuki ◽  
Kentaro Kawaguchi ◽  
Haruo Saruyama ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Tolerance ◽  
Small Heat Shock Protein ◽  
Over Expression ◽  
Rice Plants

scholarly journals Ribosome Profiling Reveals HSP90 Inhibitor Effects on Stage-Specific Protein Synthesis in Leishmania donovani

mSystems ◽  
2018 ◽  
Vol 3 (6) ◽  
Author(s):  
Eugenia Bifeld ◽  
Stephan Lorenzen ◽  
Katharina Bartsch ◽  
Juan-José Vasquez ◽  
T. Nicolai Siegel ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Leishmania Donovani ◽  
Specific Protein ◽  
Ribosome Profiling ◽  
Severe Illness ◽  
Content Type ◽  
Hsp90 Activity

ABSTRACT The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins. In the protozoan parasite Leishmania donovani, causative agent of the fatal visceral leishmaniasis, HSP90 activity is essential for cell proliferation and survival. Even more importantly, its inhibition causes life cycle progression from the insect stage to the pathogenic, mammalian stage. To unravel the molecular impact of HSP90 activity on the parasites’ gene expression, we performed a ribosome profiling analysis of L. donovani, comparing genome-wide protein synthesis patterns in the presence and absence of the HSP90-specific inhibitor radicicol and an ectopically expressed radicicol-resistant HSP90 variant. We find that ribosome-protected RNA faithfully maps open reading frames and represents 97% of the annotated protein-coding genes of L. donovani. Protein synthesis was found to correlate poorly with RNA steady-state levels, indicating a regulated translation as primary mechanism for HSP90-dependent gene expression. The results confirm inhibitory effects of HSP90 on the synthesis of Leishmania proteins that are associated with the pathogenic, intracellular stage of the parasite. Those include heat shock proteins, redox enzymes, virulence-enhancing surface proteins, proteolytic pathways, and a complete set of histones. Conversely, HSP90 promotes fatty acid synthesis enzymes. Complementing radicicol treatment with the radicicol-resistant HSP90rr variant revealed important off-target radicicol effects that control a large number of the above-listed proteins. Leishmania lacks gene-specific transcription regulation and relies on regulated translation instead. Our ribosome footprinting analysis demonstrates a controlling function of HSP90 in stage-specific protein synthesis but also significant, HSP90-independent effects of the inhibitor radicicol. IMPORTANCE Leishmania parasites cause severe illness in humans and animals. They exist in two developmental stages, insect form and mammalian form, which differ in shape and gene expression. By mapping and quantifying RNA fragments protected by protein synthesis complexes, we determined the rates of protein synthesis for >90% of all Leishmania proteins in response to the inhibition of a key regulatory protein, the 90-kDa heat shock protein. We find that Leishmania depends on a regulation of protein synthesis for controlling its gene expression and that heat shock protein 90 inhibition can trigger the developmental program from insect form to mammalian form of the pathogen.

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