ArticleMolecular and cellular biology1999
TATA-Binding protein-interacting protein 120, TIP120, stimulates three classes of eukaryotic transcription via a unique mechanism.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 36 citations in OpenAlex.
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- Article
- TIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation.BMC biochemistry · 2009Article
- Subunit compositions of the RNA-silencing enzymes Pol IV and Pol V reveal their origins as specialized forms of RNA polymerase II.Molecular cell · 2009Article
- Crystal structure of TBP-interacting protein (Tk-TIP26) and implications for its inhibition mechanism of the interaction between TBP and TATA-DNA.Protein science : a publication of the Protein Society · 2006Article
- A human-curated annotation of the Candida albicans genome.PLoS genetics · 2005Article
- Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways.Molecular and cellular biology · 2001Article
- HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions.Genome research · 2000Article
- BRCA1 can stimulate gene transcription by a unique mechanism.EMBO reports · 2000Article
- Molecular characterization of an acidic region deletion mutant of Cockayne syndrome group B protein.Nucleic acids research · 2000Article
- Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
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10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously identified a novel TATA-binding protein (TBP)-interacting protein (TIP120) from the rat liver. Here, in an RNA polymerase II (RNAP II)-reconstituted transcription system, we demonstrate that recombinant TIP120 activates the basal level of transcription from various kinds of promoters regardless of the template DNA topology and the presence of TFIIE/TFIIH and TBP-associated factors. Deletion analysis demonstrated that a 412-residue N-terminal domain, which includes an acidic region and the TBP-binding domain, is required for TIP120 function. Kinetic studies suggest that TIP120 functions during preinitiation complex (PIC) formation at the step of RNAP II/TFIIF recruitment to the promoter but not after the completion of PIC formation. Electrophoretic mobility shift assays showed that TIP120 enhanced PIC formation, and TIP120 also stimulated the nonspecific transcription and DNA-binding activity of RNAP II. These lines of evidence suggest that TIP120 is able to activate basal transcription by overcoming a kinetic impediment to RNAP II/TFIIF integration into the TBP (TFIID)-TFIIB-DNA-complex. Interestingly, TIP120 also stimulates RNAP I- and III-driven transcription and binds to RPB5, one of the common subunits of the eukaryotic RNA polymerases, in vitro. Furthermore, in mouse cells, ectopically expressed TIP120 enhances transcription from all three classes (I, II, and III) of promoters. We propose that TIP120 globally regulates transcription through interaction with basal transcription mechanisms common to all three transcription systems.
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