Strategies to Optimize Protein Expression in E. coli
Identifieur interne : 000547 ( Pmc/Curation ); précédent : 000546; suivant : 000548Strategies to Optimize Protein Expression in E. coli
Auteurs : Dana M. Francis ; Rebecca PageSource :
- Current Protocols in Protein Science [ 1934-3655 ] ; 2010.
Abstract
Recombinant protein expression in
Url:
DOI: 10.1002/0471140864.ps0524s61
PubMed: 20814932
PubMed Central: 7162232
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p>Recombinant protein expression in <named-content content-type="genus-species"><italic>Escherichia coli</italic>
</named-content>
(<named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
) is simple, fast, inexpensive, and robust, with the expressed protein comprising up to 50 percent of the total cellular protein. However, it also has disadvantages. For example, the rapidity of bacterial protein expression often results in unfolded/misfolded proteins, especially for heterologous proteins that require longer times and/or molecular chaperones to fold correctly. In addition, the highly reductive environment of the bacterial cytosol and the inability of <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
to perform several eukaryotic post‐translational modifications results in the insoluble expression of proteins that require these modifications for folding and activity. Fortunately, multiple, novel reagents and techniques have been developed that allow for the efficient, soluble production of a diverse range of heterologous proteins in <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
. This overview describes variables at each stage of a protein expression experiment that can influence solubility and offers a summary of strategies used to optimize soluble expression in <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
. <italic>Curr. Protoc. Protein Sci</italic>
. 61:5.24.1‐5.24.29. © 2010 by John Wiley & Sons, Inc.</p>
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<article-categories><subj-group subj-group-type="article-subject-classification"><subject>Biochemistry</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Protein Production, Purification, and Analysis</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Production of Recombinant Proteins</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Purification of Recombinant Proteins</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Molecular Biology</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>E. coli, Plasmids, and Bacteriophages</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Cell Culture</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Bacteria</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Bioinformatics</subject>
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<subj-group subj-group-type="article-subject-classification"><subject>Protein Analysis</subject>
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<title-group><article-title>Strategies to Optimize Protein Expression in <named-content content-type="genus-species"><italic>E. coli</italic>
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<institution>Brown University</institution>
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<volume>61</volume>
<issue>1</issue>
<issue-id pub-id-type="doi">10.1002/0471140864.2010.61.issue-1</issue-id>
<issue-title>Production of Recombinant Proteins</issue-title>
<fpage>5241</fpage>
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<permissions><pmc-comment> © John Wiley and Sons </pmc-comment>
<copyright-statement content-type="article-copyright">Copyright © 2010 John Wiley & Sons, Inc.</copyright-statement>
<license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p>
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<abstract><title>Abstract</title>
<p>Recombinant protein expression in <named-content content-type="genus-species"><italic>Escherichia coli</italic>
</named-content>
(<named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
) is simple, fast, inexpensive, and robust, with the expressed protein comprising up to 50 percent of the total cellular protein. However, it also has disadvantages. For example, the rapidity of bacterial protein expression often results in unfolded/misfolded proteins, especially for heterologous proteins that require longer times and/or molecular chaperones to fold correctly. In addition, the highly reductive environment of the bacterial cytosol and the inability of <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
to perform several eukaryotic post‐translational modifications results in the insoluble expression of proteins that require these modifications for folding and activity. Fortunately, multiple, novel reagents and techniques have been developed that allow for the efficient, soluble production of a diverse range of heterologous proteins in <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
. This overview describes variables at each stage of a protein expression experiment that can influence solubility and offers a summary of strategies used to optimize soluble expression in <named-content content-type="genus-species"><italic>E. coli</italic>
</named-content>
. <italic>Curr. Protoc. Protein Sci</italic>
. 61:5.24.1‐5.24.29. © 2010 by John Wiley & Sons, Inc.</p>
</abstract>
<kwd-group kwd-group-type="author-generated"><kwd id="cpps0524-kwd-0001">protein expression</kwd>
<kwd id="cpps0524-kwd-0002"><named-content content-type="genus-species"><italic>E. coli</italic>
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<kwd id="cpps0524-kwd-0003">fusion proteins</kwd>
<kwd id="cpps0524-kwd-0004">proteases</kwd>
<kwd id="cpps0524-kwd-0005">heterologous protein</kwd>
<kwd id="cpps0524-kwd-0006">purification tags</kwd>
<kwd id="cpps0524-kwd-0007">expression tags</kwd>
<kwd id="cpps0524-kwd-0008">expression strains and vectors</kwd>
<kwd id="cpps0524-kwd-0009">folded protein</kwd>
<kwd id="cpps0524-kwd-0010">active protein</kwd>
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