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Vol 51(2017) N 3 p. 416-425; DOI 10.1134/S0026893317020170 Full Text

N. Rai1, R. Kumar1, Md A. Haque2, Md I. Hassan2, S. Dey1*

A study of recombinant human sestrin 1 and sestrin 2 proteins produced in a prokaryotic system

1Department of Biophysics All India Institute of Medical Sciences, Ansari Nagar, New Delhi, 110029 India
2Center for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi, 110025 India

*sharmistha_d@hotmail.com
Received - 2016-01-28; Accepted - 2016-05-27

Sestrins are highly conserved stress-inducible proteins capable of suppressing the production of ROS and signalling through mTORC1. Here we report a study of human sestrin1 (sesn1) and sestrin2 (sesn2) proteins produced in a pET28+ vector based prokaryotic system. Mass spectrometry analysis, western blot and surface plasmon resonance (SPR) of affinity purified sesn1 and sesn2 proteins confirmed their identity; biophysical characteristics were observed using circular dichroism (CD) showing that sesn1 and sesn2 have a predominant α-helical structure. Here we describe a simple, one step purification process to purify a large amount of sestrin proteins with significant yield. Further study of recombinant human sestrins may further facilitate the understanding of their roles in eukaryotic cells.

Sestrin, prokaryotic system, CD, SPR



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