scholarly journals Molecular cloning, phylogenetic analysis and heat shock response of Babesia gibsoni heat shock protein 90

2016 ◽  
Vol 78 (8) ◽  
pp. 1355-1360 ◽  
Author(s):  
Masahiro YAMASAKI ◽  
Yoshihiro TSUBOI ◽  
Yusuke TANIYAMA ◽  
Naohiro UCHIDA ◽  
Reeko SATO ◽  
...  
2015 ◽  
Vol 13 (16) ◽  
pp. 4627-4631 ◽  
Author(s):  
Y. Wang ◽  
S. R. McAlpine

The cellular protection mechanism, the heat shock response, is only activated by classical heat shock 90 inhibitors (Hsp90) that “target” the N-terminus of the protein, but not by those that modulate the C-terminus.


2019 ◽  
Vol 46 (10) ◽  
pp. 925
Author(s):  
Erina Matsuoka ◽  
Naoki Kato ◽  
Masakazu Hara

The heat shock protein 90 (HSP90) inhibitor, geldanamycin, is a chemical inducer of the heat shock response (HSR) in Arabidopsis. Geldanamycin is thought to activate the heat shock signal by dissociating the HSP90-heat shock factor (HSF) complex. Recent studies have indicated that plant HSP70 is also associated with HSF, suggesting that inhibition of HSP70 may induce the HSR. However, no studies have been conducted to test this hypothesis. Here, we found that a specific HSP70 inhibitor VER-155008 activated the promoter of a small HSP gene (At1 g53540, HSP17.6C-CI) of Arabidopsis, which was shown to be activated by geldanamycin and other HSP90 inhibitors. The production of HSP17.6C-CI, HSP70 and HSP90.1 proteins in Arabidopsis was enhanced by the addition of VER-155008. The reduction of chlorophyll contents by heat shock was ameliorated by VER-155008. Chaperone analyses indicated that VER-155008 inhibited the chaperone activities of wheat germ extract and human HSP70/HSP40, respectively. These results suggest that the inhibition of HSP70 by VER-155008 enhanced the heat tolerance of Arabidopsis by inducing the HSR in the plant.


RSC Advances ◽  
2015 ◽  
Vol 5 (73) ◽  
pp. 59003-59013 ◽  
Author(s):  
Yen Chin Koay ◽  
Jeanette R. McConnell ◽  
Yao Wang ◽  
Shelli R. McAlpine

C-terminal inhibitors of heat shock protein 90 (hsp90) modulate the C-terminus and do not elicit a heat shock response.


2017 ◽  
Vol 11 (2) ◽  
pp. 107-113 ◽  
Author(s):  
Hiroki Murano ◽  
Takumi Matsubara ◽  
Ikuo Takahashi ◽  
Masakazu Hara

2002 ◽  
Vol 110 (1-2) ◽  
pp. 123-129 ◽  
Author(s):  
M Yamasaki ◽  
M Tajima ◽  
K.W Lee ◽  
J.R Jeong ◽  
O Yamato ◽  
...  

2008 ◽  
Vol 94 (1) ◽  
pp. 119-124 ◽  
Author(s):  
Masahiro Yamasaki ◽  
Motoshi Tajima ◽  
Osamu Yamato ◽  
Shiang-Jyi Hwang ◽  
Hiroshi Ohta ◽  
...  

Oncotarget ◽  
2016 ◽  
Vol 7 (20) ◽  
pp. 29648-29663 ◽  
Author(s):  
Zhixin Zhao ◽  
Jianming Zhu ◽  
Haitian Quan ◽  
Guimin Wang ◽  
Bo Li ◽  
...  

2015 ◽  
Vol 51 (8) ◽  
pp. 1410-1413 ◽  
Author(s):  
Y. Wang ◽  
S. R. McAlpine

Classic oncogenic heat shock protein 90 (Hsp90) inhibitors target the N-terminus of the protein, triggering a survival mechanism in cancer cells referred to as the heat shock response (HSR).


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