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

doi:10.7868/S0026898417020173

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 journal › Article › peer-review

3 Scopus citations

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 language	English (US)
Pages (from-to)	473-482
Number of pages	10
Journal	Molekulyarnaya Biologiya
Volume	51
Issue number	3
DOIs	https://doi.org/10.7868/S0026898417020173
State	Published - May 1 2017
Externally published	Yes

Keywords

CD
SPR
Sestrin
prokaryotic system

ASJC Scopus subject areas

General Medicine

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10.7868/S0026898417020173

Cite this

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title = "A study of recombinant human sestrin 1 and sestrin 2 proteins produced in a prokaryotic system",

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\textasciicircum{}(+) 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.",

keywords = "CD, SPR, Sestrin, prokaryotic system",

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language = "English (US)",

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journal = "Molekulyarnaya Biologiya",

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publisher = "Russian Academy of Sciences",

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TY - JOUR

T1 - A study of recombinant human sestrin 1 and sestrin 2 proteins produced in a prokaryotic system

AU - Rai, N.

AU - Kumar, R.

AU - Haque, Md A.

AU - Hassan, Md I.

AU - Dey, S.

PY - 2017/5/1

Y1 - 2017/5/1

N2 - 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.

AB - 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.

KW - CD

KW - SPR

KW - Sestrin

KW - prokaryotic system

UR - https://www.scopus.com/pages/publications/85032625797

UR - https://www.scopus.com/pages/publications/85032625797#tab=citedBy

U2 - 10.7868/S0026898417020173

DO - 10.7868/S0026898417020173

M3 - Article

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AN - SCOPUS:85032625797

SN - 0026-8984

VL - 51

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EP - 482

JO - Molekulyarnaya Biologiya

JF - Molekulyarnaya Biologiya

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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