ArticleThe Journal of biological chemistry2012
Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p and its functional implications.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 23 citations in OpenAlex.
- Context-dependent interplay of Swi-Snf and Tup1-Cyc8 influences chromatin and transcription at antagonistically regulated genes.Nature communications · 2026Article
- UBIQUITOUS FUNCTIONAL SYNERGY PARTIALLY EXPLAINS WHY MOST TRANSCRIPTION FACTOR BINDING IS NON-FUNCTIONAL.bioRxiv : the preprint server for biology · 2026Article
- A function of TPL/TBL1-type corepressors is to nucleate the assembly of the preinitiation complex.The Journal of cell biology · 2025Article
- A conserved function of corepressors is to nucleate assembly of the transcriptional preinitiation complex.bioRxiv : the preprint server for biology · 2024Article
- A single helix repression domain is functional across diverse eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Repression by theeLife · 2021Article
- Interdependent recruitment of CYC8/TUP1 and the transcriptional activator XYR1 at target promoters is required for induced cellulase gene expression in Trichoderma reesei.PLoS genetics · 2021Article
- Cyc8p and Tup1p transcription regulators antagonistically regulate Flo11p expression and complexity of yeast colony biofilms.PLoS genetics · 2018Article
- Characterisation of two Toxoplasma PROPPINs homologous to Atg18/WIPI suggests they have evolved distinct specialised functions.PloS one · 2018Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- A D53 repression motif induces oligomerization of TOPLESS corepressors and promotes assembly of a corepressor-nucleosome complex.Science advances · 2017Article
- Ssn6-Tup1 global transcriptional co-repressor: Role of the N-terminal glutamine-rich region of Ssn6.PloS one · 2017Article
- Article
- The Coprinopsis cinerea Tup1 homologue Cag1 is required for gill formation during fruiting body morphogenesis.Biology open · 2016Article
- The Unicellular Ancestry of Groucho-Mediated Repression and the Origins of Metazoan Transcription Factors.Genome biology and evolution · 2016Article
- Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors.Science advances · 2015Article
- Acquisition of the ability to assimilate mannitol by Saccharomyces cerevisiae through dysfunction of the general corepressor Tup1-Cyc8.Applied and environmental microbiology · 2015Article
- The yeast Cyc8-Tup1 complex cooperates with Hda1p and Rpd3p histone deacetylases to robustly repress transcription of the subtelomeric FLO1 gene.Biochimica et biophysica acta · 2014Article
- An evolving understanding of nuclear receptor coregulator proteins.Journal of molecular endocrinology · 2013Review
- An expanded genetic code in Candida albicans to study protein-protein interactions in vivo.Eukaryotic cell · 2013Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast Cyc8p-Tup1p protein complex is a general transcriptional corepressor of genes involved in many different physiological processes. Herein, we present the crystal structure of the Tup1p N-terminal domain (residues 1-92), essential for Tup1p self-assembly and interaction with Cyc8p. This domain tetramerizes to form a novel antiparallel four-helix bundle. Coiled coil interactions near the helical ends hold each dimer together, whereas interdimeric association involves only two sets of two residues located toward the chain centers. A mutagenesis study confirmed that the nonpolar residues responsible for the association of the protomers as dimers are also required for transcriptional repression. An additional structural study demonstrated that the domain containing an Leu(62) → Arg mutation that had been shown not to bind Cyc8p exhibits an altered structure, distinct from the wild type. This altered structure explains why the mutant cannot bind Cyc8p. The data presented herein highlight the importance of the architecture of the Tup1p N-terminal domain for self-association.
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