Linked Life Data

11790116

Source:http://linkedlifedata.com/resource/pubmed/id/11790116

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-1-15
pubmed:abstractText
We screened a human lymphocyte cDNA library using the yeast two-hybrid system and an automodification domain of PARP as a probe. The DNA sequence of an isolated clone (clone 3-9) was identical to the partial cDNA sequence of the human ribosomal protein S3a. We confirmed that PARP interacts with clone 3-9 by performing binding studies using a GST-3-9 fusion protein as bait. We also demonstrated that native S3a in nuclear extracts of HL-60 cells interacts with the automodification domain of PARP and that PARP from nuclear extracts is coprecipitated with the GST-3-9 fusion protein. Furthermore, we demonstrated that Bcl-2 interacts with PARP in association with S3a and that the interaction of S3a and Bcl-2 with PARP causes a significant decrease in PARP activity. Since Bcl-2 failed to inhibit PARP activity in the absence of S3a, we suggest that Bcl-2 together with S3a prevents apoptosis probably by inhibiting PARP activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
929-34
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Inhibition of poly(ADP-ribose) polymerase activity by Bcl-2 in association with the ribosomal protein S3a.
pubmed:affiliation
Laboratory of Molecular Biology, Medical Research Center, Kochi Medical School, Kochi 783-8505, Japan.
pubmed:publicationType
Journal Article