Literature DB >> 35089567

Optimizing Chaperone Removal Strategy from Overexpressed Recombinant Proteins : GNE, a Case Study.

Shweta Sharma1, Roop Singh Bora2, Kulvinder Singh Saini3, Ranjana Arya4.   

Abstract

In the last two decades, numerous innovative advances, strategies and protocols have been developed and optimized to improve the quality and quantity of soluble recombinant protein production in E. coli. One of the major challenges being the coelution of chaperone proteins along with desired recombinant protein of interest. The removal of chaperones is important for protein yield, structural determination, optimal activity, and desired function of the recombinant protein. In this chapter, we outline various strategies for removal of chaperone contaminants from oligomeric proteins, with the ultimate objective of ameliorating the quality and proper folding of recombinant proteins. We have discussed in detail the purification and expression of full-length protein, GNE (UDP-N-acetylglucosamine 2-epimerase/ N-acetylmannosamine kinase), as a case study for chaperone removal.
© 2022. Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Chaperones; DnaK; GST Cleanser Protein; Protein solubility

Mesh：

Substances：

Year:  2022        PMID： 35089567     DOI： 10.1007/978-1-0716-1859-2_20

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


  26 in total

1.  Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli.

Authors:  F Hoffmann; U Rinas
Journal:  Biotechnol Prog       Date:  2000 Nov-Dec

Review 2.  Molecular chaperones in the cytosol: from nascent chain to folded protein.

Authors:  F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Science       Date:  2002-03-08       Impact factor: 47.728

Review 3.  Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies.

Authors:  Sudhir Sahdev; Sunil K Khattar; Kulvinder Singh Saini
Journal:  Mol Cell Biochem       Date:  2007-09-12       Impact factor: 3.396

4.  Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries.

Authors:  S Rüdiger; L Germeroth; J Schneider-Mergener; B Bukau
Journal:  EMBO J       Date:  1997-04-01       Impact factor: 11.598

5.  A novel method for removing contaminant Hsp70 molecular chaperones from recombinant proteins.

Authors:  Enrique S Morales; Ivana L Parcerisa; Eduardo A Ceccarelli
Journal:  Protein Sci       Date:  2019-02-20       Impact factor: 6.725

Review 6.  Bacterial Heat Shock Protein Activity.

Authors:  Farajollah Maleki; Afra Khosravi; Ahmad Nasser; Hamid Taghinejad; Mitra Azizian
Journal:  J Clin Diagn Res       Date:  2016-03-01

Review 7.  Recombinant protein folding and misfolding in Escherichia coli.

Authors:  François Baneyx; Mirna Mujacic
Journal:  Nat Biotechnol       Date:  2004-11       Impact factor: 54.908

Review 8.  Production of prone-to-aggregate proteins.

Authors:  Mario Lebendiker; Tsafi Danieli
Journal:  FEBS Lett       Date:  2013-11-06       Impact factor: 4.124

9.  The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3).

Authors:  Laurence Dumon-Seignovert; Guillaume Cariot; Laurent Vuillard
Journal:  Protein Expr Purif       Date:  2004-09       Impact factor: 1.650

10.  Improved designs for pET expression plasmids increase protein production yield in Escherichia coli.

Authors:  Patrick J Shilling; Kiavash Mirzadeh; Alister J Cumming; Magnus Widesheim; Zoe Köck; Daniel O Daley
Journal:  Commun Biol       Date:  2020-05-07
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