Linked Life Data

6313206

Source:http://linkedlifedata.com/resource/pubmed/id/6313206

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-12-17
pubmed:abstractText
We have combined molecular genetic and cell-free reconstitution approaches to study the mechanism of membrane assembly. The coding region for the carboxy-terminal transmembrane sequence of membrane IgM heavy chain has been inserted between the coding regions for lactamase and globin domains of a fusion protein previously shown to be completely translocated across microsomal membranes in a cell-free transcription-linked translation system. The resulting fusion protein behaves as an integral transmembrane protein of predicted asymmetry: all of the membrane integrated copies display lactamase within the lumen and globin on the cytoplasmic face of the vesicles. In another construction, this transmembrane coding region replaces that of the signal sequence. The resulting fusion protein is not translocated across membranes. These data provide strong evidence that there are stop transfer sequences whose ability to arrest chain translocation and achieve asymmetric transmembrane orientation is independent of the size of the subsequent carboxy-terminal domain to be localized in the cytosol; and that signal and stop transfer sequences are functionally distinct.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
759-66
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
A stop transfer sequence confers predictable transmembrane orientation to a previously secreted protein in cell-free systems.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't