Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it>
<p>Abstract</p> <p>Despite the fundamental importance of <it>E. coli </it>in the manufacture of a wide range of biotechnological and biomedical products, extensive process and/or target optimisation is routinely required in order to achieve functional yields in excess o...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2009-01-01
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| Series: | Microbial Cell Factories |
| Online Access: | http://www.microbialcellfactories.com/content/8/1/9 |
| _version_ | 1818562465459339264 |
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| author | Robin Sylvain Spada Stefania Kolaj Olga Wall J Gerard |
| author_facet | Robin Sylvain Spada Stefania Kolaj Olga Wall J Gerard |
| author_sort | Robin Sylvain |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Despite the fundamental importance of <it>E. coli </it>in the manufacture of a wide range of biotechnological and biomedical products, extensive process and/or target optimisation is routinely required in order to achieve functional yields in excess of low mg/l levels. Molecular chaperones and folding catalysts appear to present a panacea for problems of heterologous protein folding in the organism, due largely to their broad substrate range compared with, <it>e.g</it>., protein-specific mutagenesis approaches. Painstaking investigation of chaperone overproduction has, however, met with mixed – and largely unpredictable – results to date. The past 5 years have nevertheless seen an explosion in interest in exploiting the native folding modulators of <it>E. coli</it>, and particularly cocktails thereof, driven largely by the availability of plasmid systems that facilitate simultaneous, non-rational screening of multiple chaperones during recombinant protein expression. As interest in using <it>E. coli </it>to produce recombinant membrane proteins and even glycoproteins grows, approaches to reduce aggregation, delay host cell lysis and optimise expression of difficult-to-express recombinant proteins will become even more critical over the coming years. In this review, we critically evaluate the performance of molecular chaperones and folding catalysts native to <it>E. coli </it>in improving functional production of heterologous proteins in the bacterium and we discuss how they might best be exploited to provide increased amounts of correctly-folded, active protein for biochemical and biophysical studies.</p> |
| first_indexed | 2024-12-14T01:04:06Z |
| format | Article |
| id | doaj.art-b2d1d85dc3104994a6466b0f0a72c26e |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-12-14T01:04:06Z |
| publishDate | 2009-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-b2d1d85dc3104994a6466b0f0a72c26e2022-12-21T23:23:05ZengBMCMicrobial Cell Factories1475-28592009-01-0181910.1186/1475-2859-8-9Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it>Robin SylvainSpada StefaniaKolaj OlgaWall J Gerard<p>Abstract</p> <p>Despite the fundamental importance of <it>E. coli </it>in the manufacture of a wide range of biotechnological and biomedical products, extensive process and/or target optimisation is routinely required in order to achieve functional yields in excess of low mg/l levels. Molecular chaperones and folding catalysts appear to present a panacea for problems of heterologous protein folding in the organism, due largely to their broad substrate range compared with, <it>e.g</it>., protein-specific mutagenesis approaches. Painstaking investigation of chaperone overproduction has, however, met with mixed – and largely unpredictable – results to date. The past 5 years have nevertheless seen an explosion in interest in exploiting the native folding modulators of <it>E. coli</it>, and particularly cocktails thereof, driven largely by the availability of plasmid systems that facilitate simultaneous, non-rational screening of multiple chaperones during recombinant protein expression. As interest in using <it>E. coli </it>to produce recombinant membrane proteins and even glycoproteins grows, approaches to reduce aggregation, delay host cell lysis and optimise expression of difficult-to-express recombinant proteins will become even more critical over the coming years. In this review, we critically evaluate the performance of molecular chaperones and folding catalysts native to <it>E. coli </it>in improving functional production of heterologous proteins in the bacterium and we discuss how they might best be exploited to provide increased amounts of correctly-folded, active protein for biochemical and biophysical studies.</p>http://www.microbialcellfactories.com/content/8/1/9 |
| spellingShingle | Robin Sylvain Spada Stefania Kolaj Olga Wall J Gerard Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> Microbial Cell Factories |
| title | Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> |
| title_full | Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> |
| title_fullStr | Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> |
| title_full_unstemmed | Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> |
| title_short | Use of folding modulators to improve heterologous protein production in <it>Escherichia coli</it> |
| title_sort | use of folding modulators to improve heterologous protein production in it escherichia coli it |
| url | http://www.microbialcellfactories.com/content/8/1/9 |
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