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Tailoring Escherichia coli for the L-Rhamnose P-BAD Promoter-Based Production of Membrane and Secretory Proteins
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 7
2017 (English)In: ACS Photonics, ISSN 2186-2311, E-ISSN 2161-5063, Vol. 6, no 6, 985-994 p.Article in journal (Refereed) Published
Abstract [en]

Membrane and secretory protein production in Escherichia coli requires precisely controlled production rates to avoid the deleterious saturation of their biogenesis pathways. On the basis of this requirement, the E. coli L-rhamnose PBAD promoter (PrhaBAD) is often used for membrane and secretory protein production since PrhaBAD is thought to regulate protein production rates in an L-rhamnose concentration-dependent manner. By monitoring protein production in real-time in E. coli wild-type and an L-rhamnose catabolism deficient mutant, we demonstrate that the L-rhamnose concentration-dependent tunability of PrhaBAD-mediated protein production is actually due to L-rhamnose consumption rather than regulating production rates. Using this information, a RhaT-mediated L-rhamnose transport and L-rhamnose catabolism deficient double mutant was constructed. We show that this mutant enables the regulation of PrhaBAD-based protein production rates in an L-rhamnose concentration-dependent manner and that this is critical to optimize membrane and secretory protein production yields. The high precision of protein production rates provided by the PrhaBAD promoter in an L-rhamnose transport and catabolism deficient background could also benefit other applications in synthetic biology.

Place, publisher, year, edition, pages
2017. Vol. 6, no 6, 985-994 p.
Keyword [en]
E. coli, protein production, L-rhamnose promoter, L-rhamnose metabolism, membrane protein, secretory protein
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-145244DOI: 10.1021/acssynbio.6b00321ISI: 000403864900008PubMedID: 28226208OAI: oai:DiVA.org:su-145244DiVA: diva2:1128666
Available from: 2017-07-27 Created: 2017-07-27 Last updated: 2017-07-27Bibliographically approved

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Karyolaimos, AlexandrosZhang, Zhede Gier, Jan-Willem
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