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

Abstract：

:We examined expression of two plant genes encoding coclaurine N-methyltransferase (CMT) and norcoclaurine synthase (NCS) in Escherichia coli from the Salmonella entericaprpBCDE promoter (P(prpB)) 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(prpB) 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.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Lee SK,Keasling JD

doi

10.1016/j.pep.2008.06.008

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

197-203

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(08)00166-6

journal_volume

61

pub_type

杂志文章

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