Heat shock Hsp70 protein is chloroplast-encoded in the chromophytic alga Pavlova lutherii

1992 ◽  
Vol 18 (3) ◽  
pp. 467-476 ◽  
Author(s):  
Carol D. Scaramuzzi ◽  
Harold W. Stokes ◽  
Roger G. Hiller
Keyword(s):  
Heat Shock ◽  
Hsp70 Protein ◽  
Chromophytic Alga

scholarly journals Comparative modeling and mutual docking of structurally uncharacterized heat shock protein 70 and heat shock factor-1 proteins in water buffalo

2019 ◽  
Vol 12 (12) ◽  
pp. 2036-2045 ◽  
Author(s):  
Ravinder Singh ◽  
Ankita Gurao ◽  
C. Rajesh ◽  
S. K. Mishra ◽  
Saroj Rani ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Heat Shock ◽  
Secondary Structure ◽  
Hydrogen Bonds ◽  
Heat Shock Protein 70 ◽  
Comparative Modeling ◽  
Side Chain ◽  
Heat Shock Factor 1 ◽  
Multiple Sequence ◽  
Hsp70 Protein

Aim: In this study, a wide range of in silico investigation of Bubalus bubalis (BB) heat shock protein 70 (HSP70) and heat shock factor-1 (HSF1) has been performed, ranging from sequence evaluation among species to homology modeling along with their docking studies to decipher the interacting residues of both molecules. Materials and Methods: Protein sequences of BB HSP70 and HSF1 were retrieved from NCBI database in FASTA format. Primary and secondary structure prediction were computed using Expasy ProtParam server and Phyre2 server, respectively. TMHMM server was used to identify the transmembrane regions in HSP70. Multiple sequence alignment and comparative analysis of the protein was carried out using MAFFT and visualization was created using ESPript 3.0. Phylogenetic analysis was accomplished by COBALT. Interactions of HSP70 with other proteins were studied using STRING database. Modeller 9.18, RaptorX, Swiss-Modeller, Phyre2, and I-TASSER were utilized to design the three-dimensional structure of these proteins followed by refinement; energy minimization was accomplished using ModRefiner and SPDBV program. Stereochemical quality along with the accuracy of the predicted models and their visualization was observed by PROCHECK program of PDBsum and UCSF Chimera, respectively. ClusPro 2.0 server was accessed for the docking of the receptor protein with the ligand. Results: The lower value of Grand Average of Hydropathy indicates the more hydrophilic nature of HSP70 protein. Value of the instability index (II) classified the protein as stable. No transmembrane region was reported for HSP70 by TMHMM server. Phylogenetic analysis based on multiple sequence alignments (MSAs) by COBALT indicated more evolutionarily closeness of Bos indicus (BI) with Bos taurus as compared to BI and BB. STRING database clearly indicates the HSF1 as one of the interacting molecules among 10 interacting partners with HSP 70. The best hit of 3D model of HSP70 protein and HSF1 was retrieved from I-TASSER and Phyre2, respectively. Interacting residues and type of bonding between both the molecules which were docked by ClusPro 2.0 were decoded by PIC server. Hydrophobic interactions, protein-protein main-chain-side-chain hydrogen bonds, and protein-protein side-chain-side-chain hydrogen bonds were delineated in this study. Conclusion: This is the first-ever study on in silico interaction of HSP70 and HSF1 proteins in BB. Several bioinformatics web tools were utilized to study secondary structure along with comparative modeling, physicochemical properties, and protein-protein interaction. The various interacting amino acid residues of both proteins have been indicated in this study.

scholarly journals Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein

1985 ◽  
Vol 5 (12) ◽  
pp. 3476-3483
Author(s):  
K O'Malley ◽  
A Mauron ◽  
J D Barchas ◽  
L Kedes
Keyword(s):  
Heat Shock ◽  
Cdna Clone ◽  
Sequence Similarity ◽  
Normal Growth ◽  
Antigenic Determinants ◽  
Related Sequence ◽  
Recombinant Clone ◽  
Hsp70 Protein ◽  
Pheochromocytoma Cell ◽  
Catecholamine Synthesizing Enzymes

A nearly full-length cDNA clone isolated from the rat pheochromocytoma cell line, PC12, revealed extensive nucleotide sequence similarity between the rat cDNA and the Drosophila melanogaster hsp70 gene. The rat recombinant clone encodes a 71,000-dalton protein that is 70% identical with the dipteran hsp70 protein. Remarkably, a truncated segment of this cDNA clone was originally isolated by immunoreactivity with antisera raised to catecholamine-synthesizing enzymes, suggesting that this heat shock protein and these catecholamine enzymes shared antigenic determinants. The rat hsp70-related mRNA is responsible for the production of a constitutive hsp70 protein, because it is present in abundant amounts in various tissues at normal growth temperatures and is only minimally induced by hyperthermia. The rat hsp70-related sequence is part of a multigene family that extends across species to mice and humans.

Heat-induced increases in endothelial NO synthase expression and activity and endothelial NO release

2003 ◽  
Vol 285 (1) ◽  
pp. H333-H340 ◽  
Author(s):  
M. Brennan Harris ◽  
Michele A. Blackstone ◽  
Hong Ju ◽  
Virginia J. Venema ◽  
Richard C. Venema
Keyword(s):  
Heat Shock ◽  
Protein Content ◽  
Heat Shock Protein 90 ◽  
Fold Increase ◽  
No Synthase ◽  
Enos Expression ◽  
Enos Activity ◽  
Hsp70 Protein ◽  
No Release ◽  
Inducible Protein

Endothelial nitric oxide (NO) synthase (eNOS) is regulated by heat shock protein 90 (HSP90), a heat-inducible protein; however, the effect of heat shock on eNOS expression and eNO release is unknown. Bovine aortic endothelial cells were incubated for 1 h at 37°C, 42°C, or 45°C and cell lysates were evaluated with the use of Western blotting. We observed a 2.1 ± 0.1-fold increase in eNOS protein content, but no change in HSP90 content, HSP70 content, or HSP90/eNOS association, 24 h after heat shock at 42°C. We also observed a 7.7 ± 1.5-fold increase in HSP70 protein content, but did not observe a change in eNOS or HSP90 24 h after heat shock at 45°C. eNOS activity and maximal bradykinin-stimulated NO release was significantly increased 24 h after heat shock at 42°C. Heat shock in rats (core temperature: 42°C, 15 min) resulted in a significant increase in aortic eNOS, HSP90, and HSP70 protein content. The aorta from heat-shocked rats exhibited a decreased maximal contractile response to phenylephrine, which was abolished by preincubation with NG-nitro-l-arginine. We conclude that prior heat shock is a physical stimulus of increased eNOS expression and is associated with an increase in eNOS activity, agonist-stimulated NO release, and a decreased vasoconstrictor response.

A deletion of the 3' end of the Drosophila melanogaster hsp70 gene increases stability of mutant mRNA during recovery from heat shock

1985 ◽  
Vol 5 (12) ◽  
pp. 3397-3402
Author(s):  
A A Simcox ◽  
C M Cheney ◽  
E P Hoffman ◽  
A Shearn
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Gene ◽  
Hsp70 Mrna ◽  
X Ray ◽  
Culture Cells ◽  
Hsp70 Protein ◽  
Tissue Culture Cells ◽  
High Level ◽  
Hsp40 Protein

hsp40, an X-ray-induced deletion mutant of the major Drosophila melanogaster heat shock protein gene hsp70, was shown to be incorrectly regulated at the translational level. hsp40 protein synthesis persisted at a high level after the release from heat shock, whereas hsp70 protein production was rapidly repressed. This result was observed both in flies heterozygous for the hsp40 gene and in tissue culture cells transfected with the truncated gene. Analysis of the transcription of the hsp40 gene indicated that its mRNA, unlike hsp70 mRNA, was not actively destabilized after a return to control temperatures, permitting prolonged production of the mutant protein.

scholarly journals Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein.

1985 ◽  
Vol 5 (12) ◽  
pp. 3476-3483 ◽  
Author(s):  
K O'Malley ◽  
A Mauron ◽  
J D Barchas ◽  
L Kedes
Keyword(s):  
Heat Shock ◽  
Cdna Clone ◽  
Sequence Similarity ◽  
Normal Growth ◽  
Antigenic Determinants ◽  
Related Sequence ◽  
Recombinant Clone ◽  
Hsp70 Protein ◽  
Pheochromocytoma Cell ◽  
Catecholamine Synthesizing Enzymes

A nearly full-length cDNA clone isolated from the rat pheochromocytoma cell line, PC12, revealed extensive nucleotide sequence similarity between the rat cDNA and the Drosophila melanogaster hsp70 gene. The rat recombinant clone encodes a 71,000-dalton protein that is 70% identical with the dipteran hsp70 protein. Remarkably, a truncated segment of this cDNA clone was originally isolated by immunoreactivity with antisera raised to catecholamine-synthesizing enzymes, suggesting that this heat shock protein and these catecholamine enzymes shared antigenic determinants. The rat hsp70-related mRNA is responsible for the production of a constitutive hsp70 protein, because it is present in abundant amounts in various tissues at normal growth temperatures and is only minimally induced by hyperthermia. The rat hsp70-related sequence is part of a multigene family that extends across species to mice and humans.

scholarly journals Heat shock protein 70 (Hsp70) is involved in the Zika virus cellular infection process

2017 ◽  
Author(s):  
Sujit Pujhari ◽  
Vanessa M. Macias ◽  
Ruth H. Nissly ◽  
Masashi Nomura ◽  
Suresh V. Kuchipudi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Zika Virus ◽  
Heat Shock Protein 70 ◽  
Membrane Surface ◽  
Infection Process ◽  
Western Hemisphere ◽  
Hsp70 Expression ◽  
Zikv Infection ◽  
Hsp70 Protein

AbstractZika virus (ZIKV) is a historically neglected flavivirus that has recently caused epidemics in the western hemisphere. ZIKV has been associated with severe symptoms including infant microcephaly and Guillain Barré syndrome, stimulating interest in understanding factors governing ZIKV infection. Heat shock protein 70 (Hsp70) has been shown to be an infection factor for multiple viruses. We investigated the role of Hsp70 in the ZIKV infection process. We localized Hsp70 protein to the Vero cell membrane surface by confocal microscopy and demonstrated that, inside the cell, there is significant co-localization between Hsp70 and ZIKV E protein. Inducing and suppressing Hsp70 expression increased and decreased ZIKV production, respectively. Antibody blocking cell surface-localized Hsp70 decreased ZIKV cell infection rates and production of infectious virus particles, as did competition with recombinant Hsp70 protein. Our data suggest that Hsp70 is an important factor in the ZIKV infection process. Understanding the interactions between Hsp70 and ZIKV may lead to novel therapeutics for ZIKV infection, particularly for pregnant women and fetuses.

scholarly journals Heat Shock Protein 40 (Hsp40) and Hsp70 Protein Expression in Oral Squamous Cell Carcinoma (OSCC)

2013 ◽  
Vol 04 (03) ◽  
pp. 734-741 ◽  
Author(s):  
Adi Prayitno ◽  
Elyana Asnar ◽  
Okid Parama Astirin ◽  
Dinar Rosmala ◽  
Suhartono Taat Putra
Keyword(s):  
Squamous Cell Carcinoma ◽  
Heat Shock ◽  
Oral Squamous Cell Carcinoma ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Cell Carcinoma ◽  
Squamous Cell ◽  
Hsp70 Protein

scholarly journals A deletion of the 3' end of the Drosophila melanogaster hsp70 gene increases stability of mutant mRNA during recovery from heat shock.

1985 ◽  
Vol 5 (12) ◽  
pp. 3397-3402 ◽  
Author(s):  
A A Simcox ◽  
C M Cheney ◽  
E P Hoffman ◽  
A Shearn
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Gene ◽  
Hsp70 Mrna ◽  
X Ray ◽  
Culture Cells ◽  
Hsp70 Protein ◽  
Tissue Culture Cells ◽  
High Level ◽  
Hsp40 Protein

hsp40, an X-ray-induced deletion mutant of the major Drosophila melanogaster heat shock protein gene hsp70, was shown to be incorrectly regulated at the translational level. hsp40 protein synthesis persisted at a high level after the release from heat shock, whereas hsp70 protein production was rapidly repressed. This result was observed both in flies heterozygous for the hsp40 gene and in tissue culture cells transfected with the truncated gene. Analysis of the transcription of the hsp40 gene indicated that its mRNA, unlike hsp70 mRNA, was not actively destabilized after a return to control temperatures, permitting prolonged production of the mutant protein.

scholarly journals Effect of 50-Hz Sinusoidal Magnetic Field on the Production of Superoxide Anion and the Expression of Heat-shock Protein 70 in RAW264 Cells

2017 ◽  
Vol 9 (2) ◽  
pp. 23 ◽  
Author(s):  
Marootpong Pooam ◽  
Maresuke Nakayama ◽  
Chihiro Nishigaki ◽  
Hidetake Miyata
Keyword(s):  
Oxidative Stress ◽  
Magnetic Field ◽  
Membrane Potential ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mitochondrial Membrane Potential ◽  
Mitochondrial Membrane ◽  
Hsp70 Protein ◽  
Enhanced Production ◽  
Sinusoidal Magnetic Field

There is a growing concern if the power-line frequency (50/60 Hz) magnetic field (termed in this paper ELF-MF) increases cancer risks. Since one of the major causes of cancer is cellular oxidative stress, whether the ELF-MF increases the oxidative stress is a central problem in the studies on the biological effect of the ELF-MF. Here, we have investigated the effect of 50-Hz sinusoidal magnetic field on the production of O2-, the expression of heat shock protein (HSP) 70 and the mitochondrial membrane potential in cell line macrophage RAW264 cells. Macrophages were exposed to or not exposed to 0.1-mT or 0.5-mT, 50-Hz sinusoidal magnetic field and were subjected to (1) assay for O2- (2) analysis of the expression of HSP70, and (3) measurement of the mitochondrial membrane potential with a fluorescent indicator. The 50-Hz magnetic field enhanced production of O2- and the expression of HSP70, both of which are consistent with previous studies. The exposure to 50-Hz magnetic field decreased mitochondrial membrane potential indicating the diminished activity of mitochondria. The uncoupler of mitochondrial function, carbonyl cyanide p-trifluoromethoxyphenylhydrazone diminished the membrane potential, as expected. On the other hand, it increased the production of O2-. The results collectively suggest that the 50-Hz magnetic field diminished the mitochondrial membrane potential, which led to the increase in the production of O2- and the expression of HSP70 protein.

scholarly journals Biochemical analysis of the stress protein response in human oesophageal epithelium

Gut ◽  
1997 ◽  
Vol 41 (2) ◽  
pp. 156-163 ◽  
Author(s):  
D Hopwood ◽  
S Moitra ◽  
B Vojtesek ◽  
D A Johnston ◽  
J F Dillon ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Stress Responses ◽  
Biochemical Analysis ◽  
Ex Vivo ◽  
Stress Protein ◽  
Hsp70 Protein ◽  
Biopsy Specimens ◽  
General Protein Synthesis ◽  
General Protein

Background—The oesophageal epithelium is exposed routinely to noxious agents in the environment, including gastric acid, thermal stress, and chemical toxins. These epithelial cells have presumably evolved effective protective mechanisms to withstand tissue damage and repair injured cells. Heat shock protein or stress protein responses play a central role in protecting distinct cell types from different types of injury.Aim—To determine (i) whether biochemical analysis of stress protein responses in pinch biopsy specimens from human oesophageal epithelium is feasible; (ii) whether undue stresses are imposed on cells by the act of sample collection, thus precluding analysis of stress responses; and (iii) if amenable to experimentation, the type of heat shock protein (Hsp) response that operates in the human oesophageal epithelium.Methods—Tissue from the human oesophagus comprised predominantly of squamous epithelium was acquired within two hours of biopsy and subjected to an in vitro heat shock. Soluble tissue cell lysates derived from untreated or heat shocked samples were examined using denaturing polyacrylamide gel electrophoresis for changes in: (i) the pattern of general protein synthesis by labelling epithelial cells with 35S-methionine and (ii) the levels of soluble Hsp70 protein and related isoforms using immunochemical protein blots.Results—A single pinch biopsy specimen is sufficient to extract and analyse specific sets of polypeptides in the oesophageal epithelium. After ex vivo heat shock, a classic inhibition of general protein synthesis is observed and correlates with the increased synthesis of two major proteins of molecular weight of 60 and 70 kDa. Notably, cells from unheated controls exhibit a “stressed” biochemical state 22 hours after incubation at 37°C, as shown by inhibition of general protein synthesis and increased synthesis of the 70 kDa protein. These data indicate that only freshly acquired specimens are suitable for studying stress responses ex vivo. No evidence was found that the two heat induced polypeptides are previously identified Hsp70 isoforms. In fact, heat shock results in a reduction in the steady state concentrations of Hsp70 protein in the oesophageal epithelium.Conclusion—Systematic and highly controlled studies on protein biochemistry are possible on epithelial biopsy specimens from the human oesophagus. These technical innovations have permitted the discovery of a novel heat shock response operating in the oesophageal epithelium. Notably, two polypeptides were synthesised after heat shock that seem to differ from Hsp70 protein. In addition, the striking reduction in steady state concentrations of Hsp70 protein after heat shock suggests that oesophageal epithelium has evolved an atypical biochemical response to thermal stress.

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