Formation of non-toxic Aβ fibrils by small heat shock protein under heat-stress conditions

2013 ◽  
Vol 430 (4) ◽  
pp. 1259-1264 ◽  
Author(s):  
Masafumi Sakono ◽  
Arata Utsumi ◽  
Tamotsu Zako ◽  
Tetsuya Abe ◽  
Masafumi Yohda ◽  
...  
1998 ◽  
Vol 116 (3) ◽  
pp. 1151-1161 ◽  
Author(s):  
Teri Chizue Suzuki ◽  
Denise C. Krawitz ◽  
Elizabeth Vierling

2020 ◽  
Vol 124 (5) ◽  
pp. 482-489
Author(s):  
Raphaela Castro Georg ◽  
Letícia Harumi Oshiquiri ◽  
Jomal Rodrigues Barbosa-Filho ◽  
Suely Lopes Gomes

HortScience ◽  
2012 ◽  
Vol 47 (1) ◽  
pp. 143-148 ◽  
Author(s):  
Yeh-Jin Ahn ◽  
Na-Hyun Song

The expression and function of DcHsp17.7, a small heat shock protein expressed in carrot (Daucus carota L.), was examined under oxidative and osmotic stress conditions. Comparative analysis revealed that DcHsp17.7 is a cytosolic Class I protein. Sequence alignment showed that DcHsp17.7 has the characteristic α-crystalline domain-containing consensus regions I and II. Under oxidative [hydrogen peroxide (H2O2)] and osmotic (polyethylene glycol) stress conditions, DcHsp17.7 accumulated in carrot leaf tissue. To examine its function under these abiotic stress conditions, the coding sequence of DcHsp17.7 was introduced into Escherichia coli and expressed by isopropyl β-D-1-thiogalactopyranoside treatment. Under both oxidative and osmotic stress conditions, heterologously expressed DcHsp17.7 enhanced bacterial cell viability. The expression level of soluble proteins was higher in transgenic cells expressing DcHsp17.7 when compared with controls under these stress conditions. These results suggest that DcHsp17.7 confers tolerance to both oxidative and osmotic stresses and thereby functions as a molecular chaperone during the stresses examined.


2012 ◽  
Vol 35 (11) ◽  
pp. 1912-1931 ◽  
Author(s):  
HARSH CHAUHAN ◽  
NEETIKA KHURANA ◽  
AASHIMA NIJHAVAN ◽  
JITENDRA P. KHURANA ◽  
PARAMJIT KHURANA

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