ArticleJournal of biosciences2003
The transcriptional activator GAL4-VP16 regulates the intra-molecular interactions of the TATA-binding protein.
Article in Journal of biosciences, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Review
- NovelInternational journal of molecular sciences · 2021Article
- Can terminators be used as insulators into yeast synthetic gene circuits?Journal of biological engineering · 2016Article
- Activation of silenced cytokine gene promoters by the synergistic effect of TBP-TALE and VP64-TALE activators.PloS one · 2014Article
- Minimal components of the RNA polymerase II transcription apparatus determine the consensus TATA box.Nucleic acids research · 2008Article
- Plant class B HSFs inhibit transcription and exhibit affinity for TFIIB and TBP.Plant molecular biology · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Binding characteristics of yeast TATA-binding protein (yTBP) over five oligomers having different TATA variants and lacking a UASGAL, showed that TATA-binding protein (TBP)-TATA complex gets stabilized in the presence of the acidic activator GAL4-VP16. Activator also greatly suppressed the non-specific TBP-DNA complex formation. The effects were more pronounced over weaker TATA boxes. Activator also reduced the TBP dimer levels both in vitro and in vivo, suggesting the dimer may be a direct target of transcriptional activators. The transcriptional activator facilitated the dimer to monomer transition and activated monomers further to help TBP bind even the weaker TATA boxes stably. The overall stimulatory effect of the GAL4-VP16 on the TBP-TATA complex formation resembles the known effects of removal of the N-terminus of TBP on its activity, suggesting that the activator directly targets the N-terminus of TBP and facilitates its binding to the TATA box.
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Registered trials
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