Genes to Cells · 2001 · 10 citations · 38 references
Life SciencesMolecular BiologyGene ExpressionTranscriptionTranscriptional RegulationRna Polymerase FunctionRna Polymerase Ii TranscriptionRna-binding ProteinsTranscription FactorsTranscription In EukaryotesTranscriptional Regulation In EukaryotesBasal Transcription MachineryFunctional Analysis Of Protein DomainsRna Polymerase Ii ActivationRna Polymerase Ii FunctionTata-box Binding ProteinTranscription Factor Binding SitesTruncation
BACKGROUND: We previously identified a TBP (TATA-binding protein)-interacting protein 120A (TIP120A) from rat liver nuclear extracts. TIP120A is thought to be a unique global transcription factor that can interact with TBP and can stimulate all classes of eukaryotic transcription. RESULTS: We produced various truncation proteins of TIP120A to delineate its functional domains. TIP120A binds to TBP in the acidic amino acid-rich N-terminal region and in the leucine-rich C-terminal region. These regions exhibited an ability to stimulate basal transcription in vitro. In addition, these two regions overlap with domains that facilitate nonspecific DNA-binding of RNA polymerase II. The sequences of these two regions are significantly conserved among TIP120A homologues of eukaryotes. CONCLUSIONS: TIP120A is a bipartite transcription factor, and both N-terminal and C-terminal regions exhibit TBP-binding activity and stimulate the basal transcription ability.
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Julie Thompson, Desmond G. Higgins, Toby J. Gibson · Nucleic Acids Research · 1994 · 64.9K citations · Full text
The Genome Sequence of <i>Drosophila melanogaster</i>
Mark D. Adams, S Celniker, Robert A. Holt et al. · Science · 2000 · 6K citations