Linked Life Data

21111764

Source:http://linkedlifedata.com/resource/pubmed/id/21111764

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-1-3
pubmed:abstractText
Dissolved oxygen (DO)-controlled nar promoter expression vectors were constructed, and their expression efficiency was compared with that of the T7 promoter pET22 expression vector by expressing human growth hormone (hGH), enhanced green fluorescence protein (EGFP), and ?-tyrosinase in Escherichia coli cells. The nar promoter expression vector pRBS, which was engineered with a 5'-untranslated region and ribosomal binding site for the T7 promoter, expressed hGH at a rate of up to 32% of the total cellular proteins (TCP) in E. coli W3110narL?. The expression level of hGH was further enhanced, up to ~42% of the TCP, by adding the N-terminal peptide tag of ?-galactosidase to hGH, which was comparable to the expression of ~43% of the TCP in pET-lac:hGH/BL21(DE3). A further engineered expression vector, pRBS(fnr), which coexpressed fumarate/nitrate reductase (fnr), expressed more EGFP than pET22 in BL21(DE3). In addition, recombinant ?-tyrosinase was successfully expressed at a rate of up to ~45% of the TCP in pRBS(fnr) in W3110narL?. From these results, the DO-controlled nar promoter system developed in this study can be considered a reliable and cost-effective expression system for protein production, especially in large-scale fermentation, as an alternative to the pET/BL(DE3) system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1873-4863
pubmed:author
pubmed:copyrightInfo
© 2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
102-7
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Development of anaerobically inducible nar promoter expression vectors for the expression of recombinant proteins in Escherichia coli.
pubmed:affiliation
Department of Chemical and Biomolecular Engineering (BK21 Program), Bioinformatics Research Center, BioProcess Engineering Research Center and Center for Ultramicrochemical Process Systems, KAIST, 335 Gwahangno, Yuseong-gu, Daejeon 305-701, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't