期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 49, 页码 37559-37565出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M608806200
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资金
- NCRR NIH HHS [RR13824] Funding Source: Medline
- NIGMS NIH HHS [U54GM074958, U54GM75026] Funding Source: Medline
We developed a new bacterial expression system that utilizes a combination of attributes ( low temperature, induction of an mRNA-specific endoribonuclease causing host cell growth arrest, and culture condensation) to facilitate stable, high level protein expression, almost 30% of total cellular protein, without background protein synthesis. With the use of an optimized vector, exponentially growing cultures could be condensed 40-fold without affecting protein yields, which lowered sample labeling costs to a few percent of the cost of a typical labeling experiment. Because the host cells were completely growth-arrested, toxic amino acids such as selenomethionine and fluorophenylalanine were efficiently incorporated into recombinant proteins in the absence of cytotoxicity. Therefore, this expression system using Escherichia coli as a bioreactor is especially well suited to structural genomics, large-scale protein expressions, and the production of cytotoxic proteins.
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