ArticleMolecular and cellular biology2000
The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49 citing papers in PubMed, 95 citations in OpenAlex.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- Histone fold domain positioning dictates cotranslational heterodimeric assembly of paralogous TAF12/TAF12L in Candida albicans.The Journal of biological chemistry · 2026Article
- Spt7 Deletion Reveals Vulnerabilities inMicroorganisms · 2026Article
- Cotranslational assembly confers specificity for in vivo target heterodimerization of paralogous H2B-like TAF12 proteins in the human fungal pathogenbioRxiv : the preprint server for biology · 2025Article
- Deletion of taf1 and taf5 in zebrafish capitulate cardiac and craniofacial abnormalities associated with TAFopathies through perturbations in metabolism.Biology open · 2023Article
- Structure of the transcription coactivator SAGA.Nature · 2020Article
- Molecular structure of promoter-bound yeast TFIID.Nature communications · 2018Article
- Reconstitution of RNA Polymerase I Upstream Activating Factor and the Roles of Histones H3 and H4 in Complex Assembly.Journal of molecular biology · 2018Article
- TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.EMBO reports · 2017Article
- Sharing the SAGA.Trends in biochemical sciences · 2017Review
- Functional specialization of two paralogous TAF12 variants by their selective association with SAGA and TFIID transcriptional regulatory complexes.The Journal of biological chemistry · 2017Article
- TAF10 Interacts with the GATA1 Transcription Factor and Controls Mouse Erythropoiesis.Molecular and cellular biology · 2015Article
- Conformational flexibility and subunit arrangement of the modular yeast Spt-Ada-Gcn5 acetyltransferase complex.The Journal of biological chemistry · 2015Article
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- Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.The EMBO journal · 2014Article
- TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.The Journal of biological chemistry · 2012Article
- Molecular evolution of the testis TAFs of Drosophila.Molecular biology and evolution · 2009Article
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- Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been previously proposed that the transcription complexes TFIID and SAGA comprise a histone octamer-like substructure formed from a heterotetramer of H4-like human hTAF(II)80 (or its Drosophila melanogaster dTAF(II)60 and yeast [Saccharomyces cerevisiae] yTAF(II)60 homologues) and H3-like hTAF(II)31 (dTAF(II)40 and yTAF(II)17) along with two homodimers of H2B-like hTAF(II)20 (dTAF(II)30alpha and yTAF(II)61/68). However, it has not been formally shown that hTAF(II)20 heterodimerizes via its histone fold. By two-hybrid analysis with yeast and biochemical characterization of complexes formed by coexpression in Escherichia coli, we showed that hTAF(II)20 does not homodimerize but heterodimerizes with hTAF(II)135. Heterodimerization requires the alpha2 and alpha3 helices of the hTAF(II)20 histone fold and is abolished by mutations in the hydrophobic face of the hTAF(II)20 alpha2 helix. Interaction with hTAF(II)20 requires a domain of hTAF(II)135 which shows sequence homology to H2A. This domain also shows homology to the yeast SAGA component ADA1, and we show that yADA1 heterodimerizes with the histone fold region of yTAF(II)61/68, the yeast hTAF(II)20 homologue. These results are indicative of a histone fold type of interaction between hTAF(II)20-hTAF(II)135 and yTAF(II)68-yADA1, which therefore constitute novel histone-like pairs in the TFIID and SAGA complexes.
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