Linked Life Data

2128597

Source:http://linkedlifedata.com/resource/pubmed/id/2128597

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-5-28
pubmed:abstractText
Bacillus subtilis neutral protease (NprE) is first produced as a precursor, pre-pro-NprE, which consists of a signal peptide or prepeptide for secretion (27 amino acid residues) and a pro-peptide (194 amino acid residues) between the signal peptide and the mature protease. While the wildtype nprE gene could not be maintained in Escherichia coli, we have been able to show that expression and secretion of the neutral protease can be achieved from the nprE gene when its ribosome binding site (RBS) is removed. The results suggest that the failure to observe expression of the wildtype nprE gene is due to the lytic effect of the nprE gene product on E. coli host cells and that translation initiation in E. coli can be achieved even in the absence of a classical ribosome binding site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:geneSymbol
nprE
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1085-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Expression in Escherichia coli of the Bacillus subtilis neutral protease gene (NPRE) lacking its ribosome binding site.
pubmed:affiliation
Department of Biochemistry, Monash University, Clayton, Victoria, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't