Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-1-22
pubmed:databankReference
pubmed:abstractText
TATA-binding protein (TBP) is a central component for transcriptional regulation and is a target for various transcription regulators. Using histidine-tagged TBP as a ligand for affinity-purification of proteins bound to TBP, we purified a 120-kD protein, termed TBP-interacting protein 120 (TIP120), from rat liver nuclear extracts. The entire cDNA sequence of TIP120 contained an open reading frame encoding a novel polypeptide of 1230 amino acids. The recombinant TIP120 interacted directly with TBP under a physiological condition in vitro. Immunoprecipitation analysis indicated that TIP120 was associated with TBP in nuclear extracts. Interestingly, the N-terminal region of TIP120 exhibited sequence similarity to that of Drosophila TAF80, which was shown to bind directly to TBP. This novel TBP-binding protein is considered to participate in transcription regulation through the interaction with TBP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
612-7
pubmed:dateRevised
2004-3-26
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Molecular cloning of a novel 120-kDa TBP-interacting protein.
pubmed:affiliation
Department of Biology, Faculty of Science, Chiba University, Japan.
pubmed:publicationType
Journal Article