Expression of low molecular weight HSP 70 related polypeptides from the symbiotic sea anemone Anemonia viridis forskall in response to heat shock

1994 ◽  
Vol 179 (2) ◽  
pp. 179-193 ◽  
Author(s):  
V.A. Sharp ◽  
D. Miller ◽  
J.C. Bythell ◽  
B.E. Brown
Marine Drugs ◽  
2018 ◽  
Vol 16 (4) ◽  
pp. 134 ◽  
Author(s):  
Erwann Loret ◽  
José Luis ◽  
Christopher Nuccio ◽  
Claude Villard ◽  
Pascal Mansuelle ◽  
...  

Author(s):  
Yukihiro Kawata ◽  
Haruhiko Fujiwara ◽  
Tadayoshi Shiba ◽  
Tadashi Miyake ◽  
Hajime Ishikawa

1985 ◽  
Vol 5 (12) ◽  
pp. 3417-3428 ◽  
Author(s):  
R T Nagao ◽  
E Czarnecka ◽  
W B Gurley ◽  
F Schöffl ◽  
J L Key

Soybeans, Glycine max, synthesize a family of low-molecular-weight heat shock (HS) proteins in response to HS. The DNA sequences of two genes encoding 17.5- and 17.6-kilodalton HS proteins were determined. Nuclease S1 mapping of the corresponding mRNA indicated multiple start termini at the 5' end and multiple stop termini at the 3' end. These two genes were compared with two other soybean HS genes of similar size. A comparison among the 5' flanking regions encompassing the presumptive HS promoter of the soybean HS-protein genes demonstrated this region to be extremely homologous. Analysis of the DNA sequences in the 5' flanking regions of the soybean genes with the corresponding regions of Drosophila melanogaster HS-protein genes revealed striking similarity between plants and animals in the presumptive promoter structure of thermoinducible genes. Sequences related to the Drosophila HS consensus regulatory element were found 57 to 62 base pairs 5' to the start of transcription in addition to secondary HS consensus elements located further upstream. Comparative analysis of the deduced amino acid sequences of four soybean HS proteins illustrated that these proteins were greater than 90% homologous. Comparison of the amino acid sequence for soybean HS proteins with other organisms showed much lower homology (less than 20%). Hydropathy profiles for Drosophila, Xenopus, Caenorhabditis elegans, and G. max HS proteins showed a similarity of major hydrophilic and hydrophobic regions, which suggests conservation of functional domains for these proteins among widely dispersed organisms.


Gene ◽  
1995 ◽  
Vol 165 (2) ◽  
pp. 223-227 ◽  
Author(s):  
Yueh-Luen Lee ◽  
Pi-Fang L. Chang ◽  
Kai-Wun Yeh ◽  
Tsung-Luo Jinn ◽  
Cheng-Che S. Kung ◽  
...  

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 851F-851 ◽  
Author(s):  
Hua Zhang ◽  
Paul H. Jennings

Heat shock was applied to 32-h-old cucumber seedlings before chilling at 2.5C. Two cultivars, `Poinsett 76' and `Ashley', with different chilling tolerances, were tested. Using root growth after chilling as a measure of chilling tolerance, three heat shock regimes were found to induce chilling tolerance in both cultivars, with the most effective and uniform induction by heat shock at 40C for 3 h. `Ashley', the more chilling tolerant cultivar, exhibited a greater response to heat shock induction of chilling tolerance than `Poinsett 76'. Protein samples from roots were subjected to SDS-PAGE. Three low molecular weight heat shock proteins accumulated to a greater extent in the protein profile of heat-shocked `Ashley' roots. No such increase was found in the `Poinsett 76' roots. The induction of low molecular weight HSPs are discussed in relation to the heat-shock induction of chilling tolerance.


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