ArticleMolecular and cellular biology2003
Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding protein.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Stress tolerance enhancement via SPT15 base editing in Saccharomyces cerevisiae.Biotechnology for biofuels · 2021Article
- An in vitro characterisation of the Trichomonas vaginalis TATA box-binding proteins (TBPs).Parasitology research · 2019Article
- Genome-wide transcriptional dependence on conserved regions of Mot1.Molecular and cellular biology · 2011Article
- The transcriptional repressor activator protein Rap1p is a direct regulator of TATA-binding protein.The Journal of biological chemistry · 2008Article
- Computer-based screening of functional conformers of proteins.PLoS computational biology · 2008Article
- A TATA binding protein regulatory network that governs transcription complex assembly.Genome biology · 2007Article
- Autonomous function of the amino-terminal inhibitory domain of TAF1 in transcriptional regulation.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The TATA binding protein (TBP) is a central component of the eukaryotic transcription machinery and is subjected to both positive and negative regulation. As is evident from structural and functional studies, TBP's concave DNA binding surface is inhibited by a number of potential mechanisms, including homodimerization and binding to the TAND domain of the TFIID subunit TAF1 (yTAF(II)145/130). Here we further characterized these interactions by creating mutations at 24 amino acids within the Saccharomyces cerevisiae TBP crystallographic dimer interface. These mutants are impaired for dimerization, TAF1 TAND binding, and TATA binding to an extent that is consistent with the crystal or nuclear magnetic resonance structure of these or related interactions. In vivo, these mutants displayed a variety of phenotypes, the severity of which correlated with relative dimer instability in vitro. The phenotypes included a low steady-state level of the mutant TBP, transcriptional derepression, dominant slow growth (partial toxicity), and synthetic toxicity in combination with a deletion of the TAF1 TAND domain. These phenotypes cannot be accounted for by defective interactions with other known TBP inhibitors and likely reflect defects in TBP dimerization.
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