Linked Life Data

20023703

Source:http://linkedlifedata.com/resource/pubmed/id/20023703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-3-25
pubmed:abstractText
The adenovirus type 5 E1B-55 kDa oncoprotein forms a complex with the tumor suppressor p53 and inactivates it. E1B-55 kDa and p53 are each capable of forming oligomers. We mapped the oligomerization domain of E1B-55 kDa to the central portion of the protein. Disturbing E1B-55 kDa self-association by point mutations at residues 285/286 or 307 not only impairs its intracellular localization to the cytoplasmic clusters, but in addition, its association with p53. Strikingly, tetramerization of p53 is also required for efficient association with E1B-55 kDa. Moreover, two different E1B-55 kDa mutants defective for p53 binding but proficient for oligomerization can trans-complement each other for p53 relocalization. We propose that the homo-oligomerization of each component enables efficient interaction between E1B-55 kDa and p53 through increased avidity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1476-5594
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1773-86
pubmed:dateRevised
2010-6-15
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Self-association of adenovirus type 5 E1B-55 kDa as well as p53 is essential for their mutual interaction.
pubmed:affiliation
Department of Molecular Oncology, Göttingen Center of Molecular Bioscience, Ernst Caspari Haus, University of Göttingen, Göttingen 37077, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't