Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-6-24
pubmed:abstractText
Protein A from Staphylococcus aureus is a powerful diagnostic reagent and has several uses in human disease therapy. Expression in non-pathogenic Escherichia coli containing recombinant plasmids coding for this protein has increased its availability, but can reduce the stability of the plasmid-bearing host. By employing immune electron microscopy, we have determined that E. coli containing stable plasmids coding for a truncated version of protein A, without the membrane binding site, secrete this protein through the cytoplasmic membrane and into the periplasmic space, where it accumulates. E. coli containing unstable plasmids, however, which code for the complete protein including the membrane-binding site, target the protein into the cytoplasmic membrane. This accumulation of protein A in the E. coli cytoplasmic membrane inhibits the formation of septa between dividing cells and results in aberrant elongated, multi-chromosomal forms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0343-8651
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
337-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The membrane binding C-terminus of protein A from Staphylococcus aureus affects its cellular localization and causes structural deformation when expressed in Escherichia coli.
pubmed:affiliation
PHLS Centre for Applied Microbiology and Research, Salisbury, UK.
pubmed:publicationType
Journal Article, Comparative Study