Literature DB >> 35089562

Applications of Cell-Free Synthesized Membrane Protein Precipitates.

Julija Mezhyrova1, Karsten Mörs1, Clemens Glaubitz1, Volker Dötsch1, Frank Bernhard2.   

Abstract

Cell-free protein expression systems are new core platforms for membrane protein synthesis. Expression in the presence of supplied artificial hydrophobic environments such as nanomembranes or micelles allows the co-translational solubilization and folding of membrane proteins. In the absence of hydrophobic compounds, the synthesized membrane proteins quantitatively precipitate, while frequently still retaining a significant part of folded structural elements. This so-called precipitate-forming cell-free (P-CF) expression mode is a very effective and reliable approach for numerous applications. Even from complex membrane proteins such as G-protein coupled receptors or large transporters, significant amounts of such precipitates can be synthesized within few hours. The precipitates can be solubilized in detergents or reconstituted into membranes for subsequent structural or functional analysis. Harsh denaturation and refolding procedures as known from the treatment of bacterial inclusion bodies are usually not required.This strategy is particularly interesting for applications requiring large amounts of membrane protein or fast access to a sample. It is further an excellent tool for the production of membrane protein antigens suitable for antibody generation. The purification of the precipitates in downstream processing is streamlined as only few proteins from the cell-free lysate may co-precipitate with the synthesized membrane protein. For most applications, a one-step affinity chromatography by taking advantage of small purification tags attached to the membrane protein target is sufficient. We give an overview on current applications of P-CF precipitates and describe the underlying techniques in detail. We furthermore provide protocols for the successful crystallization and NMR analysis of P-CF synthesized membrane proteins exemplified with the diacylglycerol kinase (DAGK). In addition, we describe the functional characterization of a P-CF synthesized large eukaryotic transporter.
© 2022. Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Cell-free protein expression; Cell-free protein precipitates; Diacylglycerol kinase (DAGK); Inclusion bodies; Membrane proteins; Organic cation transporter; P-CF mode; Solid-state NMR

Mesh:

Substances:

Year:  2022        PMID: 35089562     DOI: 10.1007/978-1-0716-1859-2_15

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


  12 in total

1.  A systematic approach to increase the efficiency of membrane protein production in cell-free expression systems.

Authors:  Stefan Haberstock; Christian Roos; Yvette Hoevels; Volker Dötsch; Gisela Schnapp; Alexander Pautsch; Frank Bernhard
Journal:  Protein Expr Purif       Date:  2012-02-08       Impact factor: 1.650

2.  Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.

Authors:  Innokentiy Maslennikov; Christian Klammt; Eunha Hwang; Georgia Kefala; Mizuki Okamura; Luis Esquivies; Karsten Mörs; Clemens Glaubitz; Witek Kwiatkowski; Young Ho Jeon; Senyon Choe
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-24       Impact factor: 11.205

3.  Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system.

Authors:  Christian Klammt; Daniel Schwarz; Klaus Fendler; Winfried Haase; Volker Dötsch; Frank Bernhard
Journal:  FEBS J       Date:  2005-12       Impact factor: 5.542

4.  Strategies for the cell-free expression of membrane proteins.

Authors:  Sina Reckel; Solmaz Sobhanifar; Florian Durst; Frank Löhr; Vladimir A Shirokov; Volker Dötsch; Frank Bernhard
Journal:  Methods Mol Biol       Date:  2010

5.  Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification.

Authors:  Parthasarathi Rath; Pascal Demange; Olivier Saurel; Marielle Tropis; Mamadou Daffé; Volker Dötsch; Alexandre Ghazi; Frank Bernhard; Alain Milon
Journal:  J Biol Chem       Date:  2011-07-28       Impact factor: 5.157

6.  High level cell-free expression and specific labeling of integral membrane proteins.

Authors:  Christian Klammt; Frank Löhr; Birgit Schäfer; Winfried Haase; Volker Dötsch; Heinz Rüterjans; Clemens Glaubitz; Frank Bernhard
Journal:  Eur J Biochem       Date:  2004-02

7.  Cell free expression and functional reconstitution of eukaryotic drug transporters.

Authors:  Thorsten Keller; Daniel Schwarz; Frank Bernhard; Volker Dötsch; Carola Hunte; Valentin Gorboulev; Hermann Koepsell
Journal:  Biochemistry       Date:  2008-03-25       Impact factor: 3.162

8.  Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination.

Authors:  Coilín Boland; Dianfan Li; Syed Tasadaque Ali Shah; Stefan Haberstock; Volker Dötsch; Frank Bernhard; Martin Caffrey
Journal:  Cell Mol Life Sci       Date:  2014-07-11       Impact factor: 9.261

9.  Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.

Authors:  Paul J Focke; Christopher Hein; Beate Hoffmann; Kimberly Matulef; Frank Bernhard; Volker Dötsch; Francis I Valiyaveetil
Journal:  Biochemistry       Date:  2016-07-21       Impact factor: 3.162

10.  Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes.

Authors:  Lei Kai; Ralf Kaldenhoff; Jiazhang Lian; Xiangcheng Zhu; Volker Dötsch; Frank Bernhard; Peilin Cen; Zhinan Xu
Journal:  PLoS One       Date:  2010-09-24       Impact factor: 3.240

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