Linked Life Data

7473745

Source:http://linkedlifedata.com/resource/pubmed/id/7473745

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-12-26
pubmed:abstractText
The activity of the catalytic alpha subunits of protein kinase CK2 is modulated by interaction with the regulatory beta subunits. In order to define the domains involved in intersubunit contacts, we have applied the two-hybrid system, which a is yeast-based genetic method for the detection of protein-protein interactions in vivo. The data demonstrate that the alpha and beta subunits interact with each other and that the beta subunits, but not the alpha subunits, are able to self-associate. This suggests that the beta subunits play a bridging role in the architecture of the CK2 holoenzyme by linking two alpha:beta heterodimers into a tetrameric complex. Analysis of truncated alpha and beta subunits was used to delimit the subregions necessary for complex formation. The data reveal that the beta subunit is modular in structure, with the two fully separable domains involved in homomeric beta:beta and heteromeric alpha:beta interactions, respectively. Also, beta subunits lacking the autophosphorylation sites in the N termini are able to associate with both the alpha and beta subunits. Furthermore, we find that the N terminus and the evolutionarily less conserved C terminus of the alpha subunit are dispensable for establishing heterodimeric alpha:beta structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
703-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Genetic dissection of intersubunit contacts within human protein kinase CK2.
pubmed:affiliation
Department of Molecular Biology, University of Aarhus, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't