Linked Life Data

7662174

Source:http://linkedlifedata.com/resource/pubmed/id/7662174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-10-10
pubmed:abstractText
Recently we developed a method called direct interaction rescue (DIRE) for selective cloning in filamentous phage. The rescue is effected by the interaction of two heterologous proteins, one fused to the N-terminus of gene 3 adhesion protein, the other fused to the C-terminus. When heterologous fusion proteins interact with each other, gene 3 protein activity in restored thereby rescuing phage infectivity. We have used the leucine zipper of c-Jun protein as a 'bait' to select for interacting proteins from a human cDNA library. Two interacting clones were isolated, one coding for ribosomal protein L18a, a component of the large ribosomal subunit, and the other for tropomyosin, a component of the cytoskeleton. L18a contains two zipper-like domains which probably interact with c-Jun. We consider it possible that L18a (and tropomyosin) are involved in the cellular regulation of Jun protein levels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
376
pubmed:geneSymbol
c-jun
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The leucine zipper of c-Jun binds to ribosomal protein L18a: a role in Jun protein regulation?
pubmed:affiliation
Institut für Molekularbiologie II der Universität Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't