Linked Life Data

8890740

Source:http://linkedlifedata.com/resource/pubmed/id/8890740

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-12-13
pubmed:abstractText
In Escherichia coli and most other microorganisms, peptide synthesis is started at methionine start codons which are read only by N-formyl-methionine-tRNA. The formyl group is normally removed from the N-terminal Met residue of the peptide by peptide deformylase (PDF). However, it has been observed that overproduction of proteins in recombinant bacteria often yields protein products which are incompletely deformylated. Certain proteins could be poor substrates for PDF and exhibit incomplete deformylation, particularly when they are overproduced. Strains of E. coli which overproduce bovine somatotropin (BST) have a significant fraction of the BST with the formyl group retained. The PDF gene was isolated and positioned into a BST production vector in such a way that the BST and PDF genes were coexpressed. In strains containing this coexpression vector, the levels of PDF were increased and formylated BST was undetectable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Increased production of peptide deformylase eliminates retention of formylmethionine in bovine somatotropin overproduced in Escherichia coli.
pubmed:affiliation
Protiva, Monsanto Company BB3M, Chesterfield, MO 63198, USA.
pubmed:publicationType
Journal Article