Effects of dinoflagellate Gymnodinium catenatum on swimming behavior and expression of heat shock protein (hsp) genes in the brine shrimp Artemia franciscana

Harmful Algae ◽  
2021 ◽  
Vol 110 ◽  
pp. 102146
Author(s):  
Jeonghoon Han ◽  
Yeun Park ◽  
Hyeon Ho Shin ◽  
A-Young Shin ◽  
Hye-Min Kang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Brine Shrimp ◽  
Swimming Behavior ◽  
Artemia Franciscana ◽  
Hsp Genes ◽  
Gymnodinium Catenatum

scholarly journals Cyst viability and stress tolerance upon heat shock protein 70 knockdown in the brine shrimp Artemia franciscana

2020 ◽  
Vol 25 (6) ◽  
pp. 1099-1103 ◽  
Author(s):  
Mat Taib Mimi Iryani ◽  
Patrick Sorgeloos ◽  
Muhd Danish-Daniel ◽  
Min Pau Tan ◽  
Li Lian Wong ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Heat Shock Protein 70 ◽  
Brine Shrimp ◽  
Artemia Franciscana ◽  
Cyst Viability

scholarly journals Knockdown of the small heat-shock protein p26 by RNA interference modifies the diapause proteome of Artemia franciscana

2019 ◽  
Vol 97 (4) ◽  
pp. 471-479
Author(s):  
Hajer Salem Malitan ◽  
Alejandro M. Cohen ◽  
Thomas H. MacRae
Keyword(s):  
Rna Interference ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Small Heat Shock Protein ◽  
Isotopic Labeling ◽  
Artemia Franciscana ◽  
Signal Transducers ◽  
Translation Factors

Embryos of the crustacean Artemia franciscana may arrest as gastrulae, forming cysts that enter diapause, which is a state of reduced metabolism and enhanced stress tolerance. Diapausing cysts survive physiological stresses for years due, in part, to molecular chaperones. p26, a small heat-shock protein, is an abundant diapause-specific molecular chaperone in cysts, and it affects embryo development and stress tolerance. p26 is therefore thought to influence many proteins in cysts, and this study was undertaken to determine how the loss of p26 by RNA interference (RNAi) affects the diapause proteome of A. franciscana. The proteome was analyzed by shot-gun proteomics coupled to differential isotopic labeling and tandem mass spectrometry. Proteins in the diapause proteome included metabolic enzymes, antioxidants, binding proteins, structural proteins, transporters, translation factors, receptors, and signal transducers. Proteins within the diapause proteome either disappeared or were reduced in amount when p26 was knocked down, or conversely, proteins appeared or increased in amount. Those proteins that disappeared may be p26 substrates, whereas the synthesis of those proteins that appeared or increased may be regulated by p26. This study provides the first global characterization of the diapause proteome of A. franciscana and demonstrates that the sHsp p26 influences proteome composition.

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.

Enhanced accumulation of constitutive heat shock protein mRNA is an initial response of eye tissue to mild hyperthermia in vivo in adult Xenopus laevis

2002 ◽  
Vol 80 (11) ◽  
pp. 1119-1123 ◽  
Author(s):  
Adnan Ali ◽  
John J Heikkila
Keyword(s):  
Heat Shock ◽  
Xenopus Laevis ◽  
Heat Shock Protein ◽  
Specific Interaction ◽  
Initial Response ◽  
Heat Shock Element ◽  
Mrna Accumulation ◽  
Mild Hyperthermia ◽  
Hsp Genes

We have examined the effect of mild hyperthermia in vivo on heat shock transcription factor (HSF) binding activity and heat shock protein (hsp) gene expression in eye tissue of adult Xenopus laevis. A specific interaction between HSF and a synthetic oligonucleotide corresponding to the proximal heat shock element of the Xenopus hsp70B gene was greatly enhanced in eyes from hyperthermic animals compared with controls. Given these results, we examined the effect of hyperthermia in vivo on the expression of five hsp genes (hsp70, hsc70, BiP, hsp90, and hsp30) in eye tissue. Interestingly, at 28°C constitutively expressed hsp genes hsc70, BiP, and hsp90 were strongly enhanced, with further accumulation at 30°C. However, hsp70 and hsp30 mRNA accumulation were not detectable at 28°C but were strongly induced at 30°C. No enhancement of the relative levels of cytoskeletal actin mRNA was observed in the eye tissue of hyperthermic animals. These results suggest that one of the primary responses of eye tissue to hyperthermia in vivo is in the elevation of mRNAs encoding a set of constitutively expressed molecular chaperones.Key words: Xenopus, mRNA, eye, heat shock, heat shock factor.

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