Investigating the role of Hsp70 chaperone from Rutilus frisii kutum in vivo in the thermal inactivation of luciferase

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Jahangirizadeh Z.; GHAFOURI H.; SAJEDI R.H.

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Journal: JOURNAL OF CELL & TISSUE Year:2018 | Volume:9 | Issue:2 Page(s): 176-186

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Information Journal Paper

Title

Investigating the role of Hsp70 chaperone from Rutilus frisii kutum in vivo in the thermal inactivation of luciferase

Author(s)

Jahangirizadeh Z. | GHAFOURI H. | SAJEDI R.H. | Issue Writer Certificate

Keywords

Hsp70Q1

Rutilus frisii kutumQ2

luciferaseQ1

in vivoQ1

thermal inactivationQ1

Abstract

Aim: The role of Hsp70 chaperone from Rutilus frisii kutum in the thermal inactivation of luciferase in E. coli cell carrying Hsp70 and firefly luciferase was investigated. Material and Methods: Co-transformation of E. coli cell was carried out with two expression vectors containing Hsp70 and firefly luciferase. The co-transformed cells carrying Hsp70 and luciferase were expressed under optimum conditions. After adding tetracycline, the cells were then incubated for 60 min at 40, 42, 44, 46, 48 and 50° C treatments. Finally, the luminescence activity of samples was calculated. Results: After 30 min at 40 and 42° C temperatures, the luciferase activity in control samples reached almost zero, while in the co-transformed samples, about 72% and 60% of the luminance activity maintained compared with control samples (before heat treatment), and even after 60 min, up to 36% and 22% of the activity remained. Also, at 44 and 46° C temperatures in the initial times after stress, a significant difference was observed between the luciferase activity of the co-transformed and the control samples. In contrast, at 48 and 50° C temperatures, the changes of the luciferase activity of co-transformed samples were small compared with control samples even in the early stages of stress. Conclusion: The thermal aggregation of luciferase as a significant reporter protein is inhibited at high temperatures via the activity of Hsp70 in the bacterial cell, which this process can be widely used in the food and pharmaceutical industries and the providing cancer diagnostic kits.

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APA: Copy

Jahangirizadeh, Z., GHAFOURI, H., & SAJEDI, R.H.. (2018). Investigating the role of Hsp70 chaperone from Rutilus frisii kutum in vivo in the thermal inactivation of luciferase. JOURNAL OF CELL & TISSUE, 9(2 ), 176-186. SID. https://sid.ir/paper/394875/en

Vancouver: Copy

Jahangirizadeh Z., GHAFOURI H., SAJEDI R.H.. Investigating the role of Hsp70 chaperone from Rutilus frisii kutum in vivo in the thermal inactivation of luciferase. JOURNAL OF CELL & TISSUE[Internet]. 2018;9(2 ):176-186. Available from: https://sid.ir/paper/394875/en

IEEE: Copy

Z. Jahangirizadeh, H. GHAFOURI, and R.H. SAJEDI, “Investigating the role of Hsp70 chaperone from Rutilus frisii kutum in vivo in the thermal inactivation of luciferase,” JOURNAL OF CELL & TISSUE, vol. 9, no. 2 , pp. 176–186, 2018, [Online]. Available: https://sid.ir/paper/394875/en

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