Linked Life Data

2152188

Source:http://linkedlifedata.com/resource/pubmed/id/2152188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-12-10
pubmed:abstractText
This paper reports the construction of plasmids which direct the overproduction of the omega subunit of Escherichia coli RNA polymerase and the subsequent purification of omega. Useful overproduction is achieved only if the natural ribosomal binding site region of rpoZ is replaced with the ribosomal binding site region of bacteriophage T7 gene 10. Overproduction is directed by T7 RNA polymerase which is provided on a separate plasmid. omega is purified by three column steps either from the insoluble inclusion body fraction or from the soluble fractions of lysates. The final yield is approximately 2 mg omega per 10 g cells wet wt. Additionally, we found that recombinant omega is readily cleaved by an endogenous protease. Sequence analysis of the most prevalent proteolytic fragment suggested that the protease responsible was the product of the ompT gene. Cleavage of omega is greatly reduced in ompT- strains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1046-5928
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:geneSymbol
ompT, rpoZ
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Overproduction and purification of the omega subunit of Escherichia coli RNA polymerase.
pubmed:affiliation
McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.