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.

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.

scholarly journals Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe

2015 ◽  
Vol 21 (2) ◽  
pp. 327-338 ◽  
Author(s):  
Attila Glatz ◽  
Ana-Maria Pilbat ◽  
Gergely L. Németh ◽  
Katalin Vince-Kontár ◽  
Katalin Jósvay ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Schizosaccharomyces Pombe ◽  
Stress Management ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

Thermal stress defense in freshwater amphipods from contrasting habitats with emphasis on small heat shock proteins (sHSPs)

2009 ◽  
Vol 34 (6) ◽  
pp. 281-285 ◽  
Author(s):  
Maxim A. Timofeyev ◽  
Zhanna M. Shatilina ◽  
Marina V. Protopopova ◽  
Darya S. Bedulina ◽  
Vasiliy V. Pavlichenko ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Freshwater Amphipods ◽  
Contrasting Habitats ◽  
Shock Proteins ◽  
Stress Defense

scholarly journals The molecular evolution of the small heat-shock proteins in plants.

Genetics ◽  
1995 ◽  
Vol 141 (2) ◽  
pp. 785-795 ◽  
Author(s):  
E R Waters
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Cellular Localization ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Gene Families ◽  
Small Heat Shock Proteins ◽  
Amino Acid Sequences ◽  
Shock Proteins

Abstract The small heat-shock proteins have undergone a tremendous diversification in plants; whereas only a single small heat-shock protein is found in fungi and many animals, over 20 different small heat-shock proteins are found in higher plants. The small heat-shock proteins in plants have diversified in both sequence and cellular localization and are encoded by at least five gene families. In the study, 44 small heat-shock protein DNA and amino acid sequences were examined, using both phylogenetic analysis and analysis of nucleotide substitution patterns to elucidate the evolutionary history of the small heat-shock proteins. The phylogenetic relationships of the small heat-shock proteins, estimated using parsimony and distance methods, reveal the gene duplication, sequence divergence and gene conversion have all played a role in the evolution of the small heat-shock proteins. Analysis of nonsynonymous substitutions and conservative and radical replacement substitutions )in relation to hydrophobicity) indicates that the small heat-shock protein gene families are evolving at different rates. This suggests that the small heat-shock proteins may have diversified in function as well as in sequence and cellular localization.

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