Temperature stress induces notochord abnormalities and heat shock proteins expression in larval green sturgeon (Acipenser medirostris Ayres 1854)

2013 ◽  
Vol 29 (5) ◽  
pp. 958-967 ◽  
Author(s):  
J. Linares-Casenave ◽  
I. Werner ◽  
J. P. Van Eenennaam ◽  
S. I. Doroshov
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Temperature Stress ◽  
Green Sturgeon ◽  
Acipenser Medirostris ◽  
Shock Proteins

scholarly journals Comparative analysis of the molecular mechanism of heat shock proteins from pathogenic and non-pathogenic E.coli

2020 ◽  
Author(s):  
Sanchari Bhattacharjee ◽  
Mohana Saha ◽  
Rakhi Dasgupta ◽  
Angshuman Bagchi
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Temperature Stress ◽  
Small Heat Shock Proteins ◽  
Lon Protease ◽  
E Coli ◽  
Physiological Temperature ◽  
Mechanism Of Interaction ◽  
Shock Proteins ◽  
Catalytic Dyad

AbstractCells can withstand the effects of temperature stress by activating small heat shock proteins IbpA and IbpB. Lon protease employing Ser679 – Lys722 catalytic dyad proteolyze IbpA and IbpB in their free forms, at physiological temperature i.e. without any temperature stress. However, the proteolytic activity of IbpA and IbpB is affected when the catalytic dyad residue of Lon protease is mutated. The mutation S679A in Lon protease brings about some changes so that the proteolytic interactions between the small heat shock proteins with that of the mutant Lon protease are lost which makes a difference in the interaction pattern of mutant Lon protease with their substrates. In the present study, we made an attempt through in-silico approach to figure out the underlying aspects of the interactions between the small heat shock proteins IbpA and IbpB with mutant Lon protease in Escherichia coli. We have tried to decipher the molecular details of the mechanism of interaction of proteolytic machinery of small heat shock proteins and mutant Lon protease with S679A mutation at physiological temperature in absence cellular temperature stress. Our study may therefore be helpful to decode the mechanistic details of the correlation with IbpA, IbpB and S679A mutant Lon protease in E. coli.

Changes in Hematological Parameters and Heat Shock Proteins in Juvenile Sablefish Depending on Water Temperature Stress

2019 ◽  
Vol 31 (2) ◽  
pp. 147-153 ◽  
Author(s):  
Jun‐Hwan Kim ◽  
Hee‐Ju Park ◽  
Do‐Hyung Kim ◽  
Chul Woong Oh ◽  
Jung Sick Lee ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Water Temperature ◽  
Temperature Stress ◽  
Hematological Parameters ◽  
Shock Proteins

scholarly journals Characterization of genes encoding small heat shock proteins from Bemisia tabaci and expression under thermal stress

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e6992 ◽  
Author(s):  
Jing Bai ◽  
Xiao-Na Liu ◽  
Ming-Xing Lu ◽  
Yu-Zhou Du
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Temperature Stress ◽  
Bemisia Tabaci ◽  
Stress Proteins ◽  
Plant Viruses ◽  
Small Heat Shock Proteins ◽  
Amino Acid Sequences ◽  
Shock Proteins

Small heat shock proteins (sHSPs) are probably the most diverse in structure and function among the various super-families of stress proteins, and they play essential roles in various biological processes. The sweet potato whitefly, Bemisia tabaci (Gennadius), feeds in the phloem, transmits several plant viruses, and is an important pest on cotton, vegetables and ornamentals. In this research, we isolated and characterized three α-crystallin/sHSP family genes (Bthsp19.5, Bthsp19.2, and Bthsp21.3) from Bemisia tabaci. The three cDNAs encoded proteins of 171, 169, and 189 amino acids with calculated molecular weights of 19.5, 19.2, and 21.3 kDa and isoelectric points of 6.1, 6.2, and 6.0, respectively. The deduced amino acid sequences of the three genes showed strong similarity to sHSPs identified in Hemiptera and Thysanoptera insects species. All three sHSPs genes from Bemisia tabaci lacked introns. Quantitative real-time PCR analyses revealed that the three BtsHSPs genes were significantly up-regulated in Bemisia tabaci adults and pupae during high temperature stress (39, 41, 43, and 45 °C) but not in response to cold temperature stress (−6, −8, −10, and −12 °C). The expression levels of Bthsp19.2 and Bthsp21.3 in pupae was higher than adults in response to heat stress, while the expression level of Bthsp19.5 in adults was higher than pupae. In conclusion, this research results show that the sHSP genes of Bemisia tabaci had shown differential expression changes under thermal stress.

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