Linked Life Data

15887232

Source:http://linkedlifedata.com/resource/pubmed/id/15887232

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-6-1
pubmed:abstractText
Interplay of the HIV-1 regulatory protein, Tat, with several cellular factors plays an important role in transcriptional regulation of the viral promoter, the long terminal repeat (LTR). Special attention has been paid to NF-kappaB, a family of inducible transcription factors, which interact with a specific DNA motif within the LTR. Here, we report on the physical and functional interaction of NFBP, a recently identified protein that interacts with the P65 subunit of NF-kappaB, with HIV-1 Tat. NFBP colocalizes with Tat in the nucleus and nucleoli, recognizes the amino acid residues 37 to 48 of Tat, and its interaction is modulated by RNA molecules. The interaction of NFBP with Tat modulates the synergism between Tat and P65 in activating LTR transcription. In the absence of the kappaB-binding sites, NFBP augments the TAR-dependent activation by Tat, yet it interferes with the synergistic effect of P65 and Tat on LTR transcription.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9541
pubmed:author
pubmed:copyrightInfo
(c) 2005 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
204
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
375-80
pubmed:dateRevised
2010-8-13
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Interplay between NFBP and NF-kappaB modulates tat activation of the LTR.
pubmed:affiliation
Center for Neurovirology and Cancer Biology, Temple University, Philadelphia, Pennsylvania, USA. sweet@temple.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural