Linked Life Data

9537509

Source:http://linkedlifedata.com/resource/pubmed/id/9537509

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-4-21
pubmed:abstractText
We isolated several clones from a matchmaker two-hybrid system human lymphocyte cDNA library using an automodification domain of poly(ADP-ribose) synthetase (PARS) as a probe. A DNA sequence (approximately 1 kbp) of the clone was identical to part of the Oct-1 DNA sequence. We then constructed either a His-tagged or GST fusion protein of the inserted cDNA from the clone and the fusion protein was shown to interact with PARS by far-Western blot analysis and co-precipitation with affinity resin. Furthermore, the His-tagged Oct-1/POU-homeo fusion protein interacted weakly with the octamer motif of the DRa promoter and the addition of PARS fusion protein greatly increased the DNA binding activity. These results suggest that PARS interacts with Oct-1 and stabilizes the binding of Oct-1 to the octamer motif.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
424
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase.
pubmed:affiliation
Laboratory of Molecular Biology, Medical Research Center, Kochi Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't