scholarly journals Functional Variation of Two Novel Cellulases, Pv-eng-5 and Pv-eng-8, and the Heat Shock 90 Gene, Pv-hsp-90, in Pratylenchus vulnus and Their Expression in Response to Different Temperature Stress

2018 ◽  
Vol 20 (1) ◽  
pp. 107
Author(s):  
Elena Fanelli ◽  
Alberto Troccoli ◽  
Francesca De Luca
Keyword(s):  
Heat Shock ◽  
Functional Characterization ◽  
Heat Shock Gene ◽  
Protective Mechanism ◽  
Reproduction Rate ◽  
Nematode Reproduction ◽  
Pratylenchus Vulnus ◽  
Significant Difference ◽  
Increasing Temperature ◽  
Hsp 90

Functional characterization of two novel endoglucanase genes, Pv-eng-5 and Pv-eng-8, of the root-lesion nematode Pratylenchus vulnus was carried out. In situ-hybridization experiments revealed that Pv-eng-8 transcript was localized in the pharyngeal glands. Silencing of Pv-eng-5 and Pv-eng-8 resulted in a significant reduction of expression level (52% and 67%, respectively). Furthermore, the silencing of Pv-eng-8 determined a reduction (41%) in nematode reproduction, suggesting that treated nematodes are much less able to process food. Surprisingly, no significant difference on reproduction rate was observed with Pv-eng-5 dsRNA nematodes, suggesting a neofunctionalization of Pv-eng-5 despite the high similarity with nematode endoglucanases. Pratylenchus species are poikilothermic organisms showing close relationships with the environmental temperature. The effects of different temperature ranges revealed that the reproductive potential of P. vulnus increased with increasing temperature from 23 °C to 28 °C, but no reproduction was observed at 33 °C. In real time, increasing temperature from 23 °C to 28 °C the heat shock gene Pv-hsp-90 was differentially expressed in adult stages, while the levels of the effector genes Pv-eng-1 and Pv-eng-8 in females showed no significant differences compared to those observed at 23 °C, only in males Pv-eng-8 level decreased (45%). The upregulation of Pv-hsp-90 in both adult stages suggests a protective mechanism in order to cope with unfavorable environmental conditions.

scholarly journals Functional characterization of natural variants found on the major stress inducible 70-kDa heat shock gene, HSPA1A, in humans

2018 ◽  
Vol 506 (4) ◽  
pp. 799-804 ◽  
Author(s):  
Ryan Oliverio ◽  
Peter Nguyen ◽  
Brianna Kdeiss ◽  
Sara Ord ◽  
Amanda J. Daniels ◽  
...  
Keyword(s):  
Heat Shock ◽  
Functional Characterization ◽  
Heat Shock Gene ◽  
Natural Variants ◽  
Shock Gene

scholarly journals Consequences of Atrial or Ventricular Tachypacing on the Heat Shock Proteins (HSP) level of Expression and Phosphorylation

2020 ◽  
Vol 12 (2) ◽  
Author(s):  
Matthew Shorofsky ◽  
Ange Maguy ◽  
Stanley Nattel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Canine Model ◽  
Right Atrial ◽  
Expression Levels ◽  
Significant Difference ◽  
Canine Models ◽  
Shock Proteins ◽  
Hsp 90

Background - Uncontrolled atrial fibrillation (AF) results in complex changes in the cardiomyocyte electrical and contractile functioning that promote atrial remodeling and the continuation of AF. Recently there has been a growing interest in understanding the role of heat shock proteins (HSPs), which are cytoprotective molecular chaperones, in the pathophysiology of AF. Several groups have examined HSP expression in patients with AF but have yielded mixed results. To allow for  better consistency and reproducibility between subjects, we utilized canine models to reproduce AF- promoting conditions to better investigate the role of HSPs in the pathophysiology of AF. Methods - AF  promoting conditions were simulated in canine models with fifteen adult mongrel dogs (20.6 to 36.0 kg) divided into three groups: (1) Control (n=5), (2) two week ventricular tachypacing (VTP) induced congestive heart failure (CHF) (n=5), and (3) one week atrial tachypacying (ATP) (n=5). Quick frozen right atrial free wall tissue samples were used for protein isolation and were analyzed via Western  blotting with data was expressed as a relative ratio and were analyzed using a two-tailed, unpaired t- test and significance was set at p < 0.05. The expression levels of HSP 90, 70, and 25 were studied along  with the phosphorylation status of HSP27 at serine-78. Results - We first examined the effects of the ATP and CHF heart models on the expression of a select group of HSPs via Western Blot. We found that there was no significant difference in levels of expression of HSP 90, 70, or 25 when either ATP or CHF models were compared to control canines. The phosphorylation status of HSP27 was significantly decreased in the CHF canine model when compared to control (p < 0.0111) and it tended towards a decrease in the ATP canine model when compared to control (p=0.0923). Conclusion - This study showed that even though the expression levels of HSPs may remain constant, there are protein phosphorylation and dephosphorylation events that occur in AF that may have important consequences in its pathophysiology. It is therefore necessary to investigate the full scale of HSP modifications during AF and AF-promoting conditions.

scholarly journals The Helicobacter pylori HspR-Modulator CbpA Is a Multifunctional Heat-Shock Protein

2020 ◽  
Vol 8 (2) ◽  
pp. 251
Author(s):  
Simona Pepe ◽  
Vincenzo Scarlato ◽  
Davide Roncarati
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Functional Characterization ◽  
Direct Interaction ◽  
Binding Activity ◽  
Regulatory Role ◽  
Heat Shock Gene ◽  
Dna Binding Activity ◽  
H Pylori

The medically important human pathogen Helicobacter pylori relies on a collection of highly conserved heat-shock and chaperone proteins to preserve the integrity of cellular polypeptides and to control their homeostasis in response to external stress and changing environmental conditions. Among this set of chaperones, the CbpA protein has been shown to play a regulatory role in heat-shock gene regulation by directly interacting with the master stress-responsive repressor HspR. Apart from this regulatory role, little is known so far about CbpA functional activities. Using biochemistry and molecular biology approaches, we have started the in vitro functional characterization of H. pylori CbpA. Specifically, we show that CbpA is a multifunctional protein, being able to bind DNA and to stimulate the ATPase activity of the major chaperone DnaK. In addition, we report a preliminary observation suggesting that CbpA DNA-binding activity can be affected by the direct interaction with the heat-shock master repressor HspR, supporting the hypothesis of a reciprocal crosstalk between these two proteins. Thus, our work defines novel functions for H. pylori CbpA and stimulates further studies aimed at the comprehension of the complex regulatory interplay among chaperones and heat-shock transcriptional regulators.

Tissue specificity of expression of heat shock gene ATHSP70-10 in Arabidopsis thaliana seedlings under normal and stress conditions

2020 ◽  
Vol 2020 (3) ◽  
pp. 37-47
Author(s):  
L.Ye. Kozeko ◽  
◽  
E.L. Kordyum ◽  
Keyword(s):  
Arabidopsis Thaliana ◽  
Heat Shock ◽  
Water Deficit ◽  
Tissue Specificity ◽  
Abiotic Factors ◽  
Root Apex ◽  
Stress Conditions ◽  
Heat Shock Gene ◽  
Organ Specificity ◽  
Pcr Analysis

Mitochondrial heat shock proteins of HSP70 family support protein homeostasis in mitochondria under normal and stress conditions. They provide folding and complex assembly of proteins encoded by mitochondrial genome, as well as import of cytosolic proteins to mitochondria, their folding and protection against aggregation. There are reports about organ-specificity of mitochondrial HSP70 synthesis in plants. However, tissue specificity of their functioning remains incompletely characterized. This problem was studied for mitochondrial AtHSP70-10 in Arabidopsis thaliana seedlings using a transgenic line with uidA signal gene under normal conditions, as well as high temperature and water deficit. Under normal conditions, histochemical GUS-staining revealed the expression of AtHSP70-10 in cotyledon and leaf hydathodes, stipules, central cylinder in root differentiation and mature zones, as well as weak staining in root apex and root-shoot junction zone. RT-PCR analysis of wild-type seedlings exposed to 37°C showed rapid upregulation of AtHSP70-10, which reached the highest level within 2 h. In addition, the gradual development of water deficit for 5 days caused an increase in transcription of this gene, which became more pronounced after 3 days and reached a maximum after 5 days of dehydration. Histochemical analysis showed complete preservation of tissue localization of AtHSP70-10 expression under both abiotic factors. The data obtained indicate the specific functioning of mitochondrial chaperone AtHSP70-10 in certain plant cellular structures.

scholarly journals Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La.

1988 ◽  
Vol 263 (24) ◽  
pp. 11718-11728 ◽  
Author(s):  
D T Chin ◽  
S A Goff ◽  
T Webster ◽  
T Smith ◽  
A L Goldberg
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Gene ◽  
Shock Gene
Sign in / Sign up

Export Citation Format

Share Document