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

N. Rai, R. Kumar, Md A. Haque, Md I. Hassan, S. Dey

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)473-482
Number of pages10
JournalMolekulyarnaya Biologiya
Volume51
Issue number3
DOIs
StatePublished - May 1 2017
Externally publishedYes

Keywords

  • CD
  • SPR
  • Sestrin
  • prokaryotic system

ASJC Scopus subject areas

  • General Medicine

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