Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study
Escherichia coli (E. coli) remains the most commonly used host for recombinant protein expression. It is well known that a variety of experimental factors influence the protein production level as well as the solubility profile of over-expressed proteins. This becomes increasingly important for opti...
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creator | Busso, Didier Peleg, Yoav Heidebrecht, Tatjana Romier, Christophe Jacobovitch, Yossi Dantes, Ada Salim, Loubna Troesch, Edouard Schuetz, Anja Heinemann, Udo Folkers, Gert E. Geerlof, Arie Wilmanns, Matthias Polewacz, Andrea Quedenau, Claudia Büssow, Konrad Adamson, Rachel Blagova, Elena Walton, Julia Cartwright, Jared L. Bird, Louise E. Owens, Raymond J. Berrow, Nick S. Wilson, Keith S. Sussman, Joel L. Perrakis, Anastassis Celie, Patrick H.N. |
description | Escherichia coli (E. coli) remains the most commonly used host for recombinant protein expression. It is well known that a variety of experimental factors influence the protein production level as well as the solubility profile of over-expressed proteins. This becomes increasingly important for optimizing production of protein complexes using co-expression strategies. In this study, we focus on the effect of the choice of the expression vector system: by standardizing experimental factors including bacterial strain, cultivation temperature and growth medium composition, we compare the effectiveness of expression technologies used by the partners of the Structural Proteomics in Europe 2 (SPINE2-complexes) consortium. Four different protein complexes, including three binary and one ternary complex, all known to be produced in the soluble form in E. coli, are used as the benchmark targets. The respective genes were cloned by each partner into their preferred set of vectors. The resulting constructs were then used for comparative co-expression analysis done in parallel and under identical conditions at a single site. Our data show that multiple strategies can be applied for the expression of protein complexes in high yield. While there is no ‘silver bullet’ approach that was infallible even for this small test set, our observations are useful as a guideline to delineate co-expression strategies for particular protein complexes. |
doi_str_mv | 10.1016/j.jsb.2011.03.004 |
format | Article |
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It is well known that a variety of experimental factors influence the protein production level as well as the solubility profile of over-expressed proteins. This becomes increasingly important for optimizing production of protein complexes using co-expression strategies. In this study, we focus on the effect of the choice of the expression vector system: by standardizing experimental factors including bacterial strain, cultivation temperature and growth medium composition, we compare the effectiveness of expression technologies used by the partners of the Structural Proteomics in Europe 2 (SPINE2-complexes) consortium. Four different protein complexes, including three binary and one ternary complex, all known to be produced in the soluble form in E. coli, are used as the benchmark targets. The respective genes were cloned by each partner into their preferred set of vectors. The resulting constructs were then used for comparative co-expression analysis done in parallel and under identical conditions at a single site. Our data show that multiple strategies can be applied for the expression of protein complexes in high yield. While there is no ‘silver bullet’ approach that was infallible even for this small test set, our observations are useful as a guideline to delineate co-expression strategies for particular protein complexes.</description><identifier>ISSN: 1047-8477</identifier><identifier>EISSN: 1095-8657</identifier><identifier>DOI: 10.1016/j.jsb.2011.03.004</identifier><identifier>PMID: 21382497</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Academies and Institutes ; CCAAT-Binding Factor - biosynthesis ; CCAAT-Binding Factor - genetics ; Cell Cycle Proteins - biosynthesis ; Cell Cycle Proteins - genetics ; Cloning strategies ; Cloning, Molecular - methods ; Co-expression ; Enzyme-free cloning ; Escherichia coli ; Escherichia coli - genetics ; Europe ; Gateway ; Geminin ; Genetic Vectors - standards ; In-Fusion ; International Cooperation ; Israel ; LIC ; Life Sciences ; Multiprotein Complexes - biosynthesis ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - isolation & purification ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Restriction-free cloning ; Transcription Factors, TFII - biosynthesis ; Transcription Factors, TFII - genetics</subject><ispartof>Journal of structural biology, 2011-08, Vol.175 (2), p.159-170</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-111d2f41e5dddadb2a866a9955a0bc70c20550dae935fb50b78cb7edc4841e673</citedby><cites>FETCH-LOGICAL-c429t-111d2f41e5dddadb2a866a9955a0bc70c20550dae935fb50b78cb7edc4841e673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jsb.2011.03.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21382497$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04312193$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Busso, Didier</creatorcontrib><creatorcontrib>Peleg, Yoav</creatorcontrib><creatorcontrib>Heidebrecht, Tatjana</creatorcontrib><creatorcontrib>Romier, Christophe</creatorcontrib><creatorcontrib>Jacobovitch, Yossi</creatorcontrib><creatorcontrib>Dantes, Ada</creatorcontrib><creatorcontrib>Salim, Loubna</creatorcontrib><creatorcontrib>Troesch, Edouard</creatorcontrib><creatorcontrib>Schuetz, Anja</creatorcontrib><creatorcontrib>Heinemann, Udo</creatorcontrib><creatorcontrib>Folkers, Gert E.</creatorcontrib><creatorcontrib>Geerlof, Arie</creatorcontrib><creatorcontrib>Wilmanns, Matthias</creatorcontrib><creatorcontrib>Polewacz, Andrea</creatorcontrib><creatorcontrib>Quedenau, Claudia</creatorcontrib><creatorcontrib>Büssow, Konrad</creatorcontrib><creatorcontrib>Adamson, Rachel</creatorcontrib><creatorcontrib>Blagova, Elena</creatorcontrib><creatorcontrib>Walton, Julia</creatorcontrib><creatorcontrib>Cartwright, Jared L.</creatorcontrib><creatorcontrib>Bird, Louise E.</creatorcontrib><creatorcontrib>Owens, Raymond J.</creatorcontrib><creatorcontrib>Berrow, Nick S.</creatorcontrib><creatorcontrib>Wilson, Keith S.</creatorcontrib><creatorcontrib>Sussman, Joel L.</creatorcontrib><creatorcontrib>Perrakis, Anastassis</creatorcontrib><creatorcontrib>Celie, Patrick H.N.</creatorcontrib><title>Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study</title><title>Journal of structural biology</title><addtitle>J Struct Biol</addtitle><description>Escherichia coli (E. coli) remains the most commonly used host for recombinant protein expression. It is well known that a variety of experimental factors influence the protein production level as well as the solubility profile of over-expressed proteins. This becomes increasingly important for optimizing production of protein complexes using co-expression strategies. In this study, we focus on the effect of the choice of the expression vector system: by standardizing experimental factors including bacterial strain, cultivation temperature and growth medium composition, we compare the effectiveness of expression technologies used by the partners of the Structural Proteomics in Europe 2 (SPINE2-complexes) consortium. Four different protein complexes, including three binary and one ternary complex, all known to be produced in the soluble form in E. coli, are used as the benchmark targets. The respective genes were cloned by each partner into their preferred set of vectors. The resulting constructs were then used for comparative co-expression analysis done in parallel and under identical conditions at a single site. Our data show that multiple strategies can be applied for the expression of protein complexes in high yield. 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biosynthesis</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - isolation & purification</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Restriction-free cloning</subject><subject>Transcription Factors, TFII - biosynthesis</subject><subject>Transcription Factors, TFII - genetics</subject><issn>1047-8477</issn><issn>1095-8657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9v1DAQxS0EoqXwAbig3BCHBE9ixzGcVtXSIq3EBc6WY09YL_mzeJKq--1xtKXlxGms0e89jd9j7C3wAjjUHw_Fgdqi5AAFrwrOxTN2CVzLvKmler6-hcobodQFe0V04ImAEl6yixKqphRaXTLa3h8jEoVpzKYuO8ZpxjBmbhqOPd4jZQuF8Wc2LP0c0ibbkttjDG4fbIL68I8ixycrOtGMA33KNlmLo9sPNv5afWhe_Ok1e9HZnvDNw7xiP75sv1_f5rtvN1-vN7vciVLPOQD4shOA0ntvfVvapq6t1lJa3jrFXcml5N6irmTXSt6qxrUKvRNNEtWqumIfzr5725tjDOmIk5lsMLebnVl3XFQpD13dQWLfn9n0n98L0myGQA773o44LWQaVYPmuhKJhDPp4kQUsXu0Bm7WWszBpFrMWovhlUmhJ827B_elHdA_Kv72kIDPZwBTHncBoyEXUnDoQ0Q3Gz-F_9j_AV6An3g</recordid><startdate>201108</startdate><enddate>201108</enddate><creator>Busso, Didier</creator><creator>Peleg, Yoav</creator><creator>Heidebrecht, Tatjana</creator><creator>Romier, Christophe</creator><creator>Jacobovitch, Yossi</creator><creator>Dantes, Ada</creator><creator>Salim, Loubna</creator><creator>Troesch, Edouard</creator><creator>Schuetz, Anja</creator><creator>Heinemann, Udo</creator><creator>Folkers, Gert E.</creator><creator>Geerlof, Arie</creator><creator>Wilmanns, Matthias</creator><creator>Polewacz, Andrea</creator><creator>Quedenau, Claudia</creator><creator>Büssow, Konrad</creator><creator>Adamson, Rachel</creator><creator>Blagova, Elena</creator><creator>Walton, Julia</creator><creator>Cartwright, Jared L.</creator><creator>Bird, Louise E.</creator><creator>Owens, Raymond J.</creator><creator>Berrow, Nick S.</creator><creator>Wilson, Keith S.</creator><creator>Sussman, Joel L.</creator><creator>Perrakis, Anastassis</creator><creator>Celie, Patrick H.N.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>201108</creationdate><title>Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study</title><author>Busso, Didier ; Peleg, Yoav ; Heidebrecht, Tatjana ; Romier, Christophe ; Jacobovitch, Yossi ; Dantes, Ada ; Salim, Loubna ; Troesch, Edouard ; Schuetz, Anja ; Heinemann, Udo ; Folkers, Gert E. ; Geerlof, Arie ; Wilmanns, Matthias ; Polewacz, Andrea ; Quedenau, Claudia ; Büssow, Konrad ; Adamson, Rachel ; Blagova, Elena ; Walton, Julia ; Cartwright, Jared L. ; Bird, Louise E. ; Owens, Raymond J. ; Berrow, Nick S. ; Wilson, Keith S. ; Sussman, Joel L. ; Perrakis, Anastassis ; Celie, Patrick H.N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-111d2f41e5dddadb2a866a9955a0bc70c20550dae935fb50b78cb7edc4841e673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Academies and Institutes</topic><topic>CCAAT-Binding Factor - 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subjects | Academies and Institutes CCAAT-Binding Factor - biosynthesis CCAAT-Binding Factor - genetics Cell Cycle Proteins - biosynthesis Cell Cycle Proteins - genetics Cloning strategies Cloning, Molecular - methods Co-expression Enzyme-free cloning Escherichia coli Escherichia coli - genetics Europe Gateway Geminin Genetic Vectors - standards In-Fusion International Cooperation Israel LIC Life Sciences Multiprotein Complexes - biosynthesis Multiprotein Complexes - chemistry Multiprotein Complexes - isolation & purification Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Restriction-free cloning Transcription Factors, TFII - biosynthesis Transcription Factors, TFII - genetics |
title | Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study |
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