scholarly journals Characterization of Two Small Heat Shock Protein Genes (Hsp17.4 and Hs20.3) from Sitodiplosis mosellana, and Their Expression Regulation during Diapause

Insects ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 119
Author(s):  
Jiajia Zhao ◽  
Qitong Huang ◽  
Guojun Zhang ◽  
Keyan Zhu-Salzman ◽  
Weining Cheng
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Cold Stress ◽  
Small Heat Shock Protein ◽  
Short Term ◽  
Sitodiplosis Mosellana ◽  
Severe Heat Stress ◽  
Carboxy Terminal ◽  
Shock Proteins

Sitodiplosis mosellana, a periodic but devastating wheat pest that escapes temperature extremes in summer and winter by undergoing obligatory diapause. To determine the roles of small heat shock proteins (sHsps) in diapause of S. mosellana, we characterized two sHsp genes, SmHsp17.4 and SmHsp20.3, from this species. Both SmHsps contained the conserved α-crystallin domain and the carboxy-terminal I/VXI/V motif of the sHsp family. SmHsp17.4 had one intron while SmHsp20.3 had none. Quantitative PCR revealed that SmHsp17.4 expression decreased after diapause initiation, but substantially increased during transition to post-diapause quiescence. In contrast, SmHsp20.3 expression was not affected by entry of diapause, but was clearly up-regulated during summer and winter. Short-term more severe heat-stress (≥35 °C) of over-summering larvae or cold-stress (≤−5 °C) of over-wintering larvae could stimulate higher expression of both genes, and SmHsp17.4 was more responsive to cold stress while SmHsp20.3 was more sensitive to heat stress. Notably, transcription of SmHsp17.4, but not SmHsp20.3, in diapausing larvae was inducible by 20-hydroxyecdysone (20E). Recombinant SmHsp17.4 and SmHsp20.3 proteins also displayed significant chaperone functionality. These findings suggest that both SmHsps play key roles in stress tolerance during diapause; and 20E-regulated SmHsp17.4 was also likely involved in diapause termination.

scholarly journals Effects of Short-term Acute Heat Stress on Physiological Responses and Heat Shock Proteins of Hanwoo Steer (Korean Cattle)

2019 ◽  
Vol 34 (3) ◽  
pp. 173-182
Author(s):  
Youl-Chang Baek ◽  
Minseok Kim ◽  
Jin-Young Jeong ◽  
Young-Kyoon Oh ◽  
Sung-Dae Lee ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Physiological Responses ◽  
Short Term ◽  
Korean Cattle ◽  
Acute Heat Stress ◽  
Shock Proteins

scholarly journals Short-term cold stress and heat shock proteins in the crustacean Artemia franciscana

2020 ◽  
Vol 25 (6) ◽  
pp. 1083-1097
Author(s):  
Yayra A. Gbotsyo ◽  
Nathan M. Rowarth ◽  
Laura K. Weir ◽  
Thomas H. MacRae
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cold Stress ◽  
Artemia Franciscana ◽  
Short Term ◽  
Shock Proteins

scholarly journals Molecular Characterization of hsp20, Encoding a Small Heat Shock Protein of Bifidobacterium breve UCC2003

2007 ◽  
Vol 73 (14) ◽  
pp. 4695-4703 ◽  
Author(s):  
Marco Ventura ◽  
Carlos Canchaya ◽  
Ziding Zhang ◽  
Gerald F. Fitzgerald ◽  
Douwe van Sinderen
Keyword(s):  
Heat Shock ◽  
Stress Proteins ◽  
Osmotic Shock ◽  
Small Heat Shock Protein ◽  
Bifidobacterium Breve ◽  
Class B ◽  
Close Relationship ◽  
Encoding Gene ◽  
Shock Proteins

ABSTRACT Small heat shock proteins (sHSPs) are members of a diverse family of stress proteins that are important in cells to protect proteins under stressful conditions. Genome analysis of Bifidobacterium breve UCC2003 revealed a single sHSP-encoding gene, which was classified as a hsp20 gene by comparative analyses. Genomic surveillance of available genome sequences indicated that hsp20 homologs are not widely distributed in bacteria. In members of the genus Bifidobacterium, this gene appears to be present in only 7 of the 30 currently described species. Moreover, phylogenetic analysis using all available bacterial and eukaryotic sHSP sequences revealed a close relationship between bifidobacterial HSP20 and the class B sHSPs found in members of the division Firmicutes. The results of this comparative analysis and variation in codon usage content suggest that hsp20 was acquired by certain bifidobacteria through horizontal gene transfer. Analysis by slot blot, Northern blot, and primer extension experiments showed that transcription of hsp20 is strongly induced in response to severe heat shock regimens and by osmotic shock.

scholarly journals Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus

2005 ◽  
Vol 187 (15) ◽  
pp. 5236-5241 ◽  
Author(s):  
Mieko Otani ◽  
Toshiyuki Ueki ◽  
Satoshi Kozuka ◽  
Miki Segawa ◽  
Keiji Sano ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Myxococcus Xanthus ◽  
Small Heat Shock Protein ◽  
Insertion Mutation ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
2D Gel ◽  
Shock Proteins

ABSTRACT A number of heat shock proteins in Myxococcus xanthus were previously identified by two-dimensional (2D) gel electrophoresis. One of these protein was termed Mx Hsp16.6, and the gene encoding Mx Hsp16.6 was isolated. Mx Hsp16.6 consists of 147 amino acid residues and has an estimated molecular weight of 16,642, in accordance with the apparent molecular mass in the 2D gel. An α-crystallin domain, typically conserved in small heat shock proteins, was found in Mx Hsp16.6. Mx Hsp16.6 was not detected during normal vegetative growth but was immediately induced after heat shock. Expression of the hsp16.6 gene was not induced by other stresses, such as starvation, oxidation, and high osmolarity. Mx Hsp16.6 was mostly localized in particles formed after heat shock and precipitated by low-speed centrifugation. Furthermore, Mx Hsp16.6 was detected in highly electron-dense particles in heat-shocked cells by immunoelectron microscopy, suggesting that it forms large complexes with heat-denatured proteins. An insertion mutation in the hsp16.6 gene resulted in lower viability during heat shock and lower acquired thermotolerance. Therefore, it is likely that Mx Hsp16.6 plays critical roles in the heat shock response in M. xanthus.

scholarly journals Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of ‘quasi-ordered’ states

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Amanda F Clouser ◽  
Hannah ER Baughman ◽  
Benjamin Basanta ◽  
Miklos Guttman ◽  
Abhinav Nath ◽  
...  
Keyword(s):  
Heat Shock ◽  
Hybrid Approach ◽  
Small Heat Shock Protein ◽  
Exchange Mass Spectrometry ◽  
Structure And Dynamics ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Shock Proteins ◽  
Structural Insights

Small heat shock proteins (sHSPs) are nature’s ‘first responders’ to cellular stress, interacting with affected proteins to prevent their aggregation. Little is known about sHSP structure beyond its structured α-crystallin domain (ACD), which is flanked by disordered regions. In the human sHSP HSPB1, the disordered N-terminal region (NTR) represents nearly 50% of the sequence. Here, we present a hybrid approach involving NMR, hydrogen-deuterium exchange mass spectrometry, and modeling to provide the first residue-level characterization of the NTR. The results support a model in which multiple grooves on the ACD interact with specific NTR regions, creating an ensemble of ‘quasi-ordered’ NTR states that can give rise to the known heterogeneity and plasticity of HSPB1. Phosphorylation-dependent interactions inform a mechanism by which HSPB1 is activated under stress conditions. Additionally, we examine the effects of disease-associated NTR mutations on HSPB1 structure and dynamics, leveraging our emerging structural insights.

scholarly journals Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” states

2019 ◽  
Author(s):  
Amanda F. Clouser ◽  
Hannah E.R. Baughman ◽  
Benjamin Basanta ◽  
Miklos Guttman ◽  
Abhinav Nath ◽  
...  
Keyword(s):  
Heat Shock ◽  
Hybrid Approach ◽  
Small Heat Shock Protein ◽  
Exchange Mass Spectrometry ◽  
Structure And Dynamics ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Shock Proteins ◽  
Structural Insights

ABSTRACTSmall heat shock proteins (sHPSs) are nature’s “first responders” to cellular stress, interacting with affected proteins to prevent their aggregation. Little is known about sHSP structure beyond its structured α-crystallin domain (ACD), which is flanked by disordered regions. In the human sHSP HSPB1, the disordered N-terminal region (NTR) represents nearly 50% of the sequence. Here, we present a hybrid approach involving NMR, hydrogen-deuterium exchange mass spectrometry, and modeling to provide the first residue-level characterization of the NTR. The results support a model in which multiple grooves on the ACD interact with specific NTR regions, creating an ensemble of “quasi-ordered” NTR states that can give rise to the known heterogeneity and plasticity of HSPB1. Phosphorylation-dependent interactions inform a mechanism by which HSPB1 is activated under stress conditions. Additionally, we examine the effects of disease-associated NTR mutations on HSPB1 structure and dynamics, leveraging our emerging structural insights.

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.

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