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Lee, Sung Kuk
Synthetic Biology & Metabolic Engineering Laboratory
Research Interests
  • Biofuels production
  • Gene discovery
  • Protein engineering
  • Development of gene expression systems
  • Metabolic pathway regulation
  • Metabolic pathway optimization using functional genomics
  • Synthetic biology
  • Development of biosensors

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Heterologous protein production in Escherichia coli using the propionate-inducible pPro system by conventional and auto-induction methods

Cited 11 times inthomson ciCited 12 times inthomson ci
Title
Heterologous protein production in Escherichia coli using the propionate-inducible pPro system by conventional and auto-induction methods
Author
Lee, Sung KukKeasling, Jay D.
Keywords
Auto-induction; Escherichia coli; Gene expression system; pPro system; prpBCDE promoter; T7 promoter
Issue Date
2008-10
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
PROTEIN EXPRESSION AND PURIFICATION, v.61, no.2, pp.197 - 203
Abstract
We examined expression of two plant genes encoding coclaurine N-methyltransferase (CMT) and norcoclaurine synthase (NCS) in Escherichia coli from the Salmonella enterica prpBCDE promoter (Pp,B) and compared it to that from the strongest IPTG-inducible promoter, P-T7. In contrast to our previous study showing slightly higher production of green fluorescent protein (GFP) from the pPro system compared to that from the T7 system, production of two plant proteins CMT and NCS from P-prpB was 2- to 4-fold higher than that from P-T7. Unlike P-T7, expression from P-prB did not reduce cell growth even when highly induced, indicating that this propionate-inducible system is more efficient for overproduction of proteins that result in growth inhibition. In an auto-induction experiment, which does not require monitoring the culture or adding inducer during cell growth, the pPro system exhibited much higher protein production than the T7 system. These results strongly indicate that the pPro system is well-suited for overproduction of recombinant proteins. Published by Elsevier Inc.
URI
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DOI
10.1016/j.pep.2008.06.008
ISSN
1046-5928
Appears in Collections:
ECHE_Journal Papers
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