ArticleThe Journal of biological chemistry2012
TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- Fine mapping of QTL conferring Cercospora leaf spot disease resistance in mungbean revealed TAF5 as candidate gene for the resistance.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Article
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
- Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.Current opinion in structural biology · 2020Review
- Epigenetics and transcription regulation during eukaryotic diversification: the saga of TFIID.Genes & development · 2019Article
- Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.Nature structural & molecular biology · 2018Article
- Towards a mechanistic understanding of core promoter recognition from cryo-EM studies of human TFIID.Current opinion in structural biology · 2017Review
- Structural dynamics and DNA interaction of human TFIID.Transcription · 2017Article
- Cryo-EM in the study of challenging systems: the human transcription pre-initiation complex.Current opinion in structural biology · 2016Review
- Zooming in on Transcription Preinitiation.Journal of molecular biology · 2016Review
- Article
- Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Plant physiology · 2016Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- The TAF9 C-terminal conserved region domain is required for SAGA and TFIID promoter occupancy to promote transcriptional activation.Molecular and cellular biology · 2014Article
- Transcriptional analysis of apoptotic cerebellar granule neurons following rescue by gastric inhibitory polypeptide.International journal of molecular sciences · 2014Article
- Using RNA inverse folding to identify IRES-like structural subdomains.RNA biology · 2013Article
- Article
- Structure, assembly and dynamics of macromolecular complexes by single particle cryo-electron microscopy.Journal of nanobiotechnology · 2013Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The general transcription factor TFIID recognizes specifically the core promoter of genes transcribed by eukaryotic RNA polymerase II, nucleating the assembly of the preinitiation complex at the transcription start site. However, the understanding in molecular terms of TFIID assembly and function remains poorly understood. Histone fold motifs have been shown to be extremely important for the heterodimerization of many TFIID subunits. However, these subunits display several evolutionary conserved noncanonical features when compared with histones, including additional regions whose role is unknown. Here we show that the conserved additional C-terminal region of TFIID subunit TAF6 can be divided into two domains: a small middle domain (TAF6M) and a large C-terminal domain (TAF6C). Our crystal structure of the TAF6C domain from Antonospora locustae at 1.9 Å resolution reveals the presence of five conserved HEAT repeats. Based on these data, we designed several mutants that were introduced into full-length human TAF6. Surprisingly, the mutants affect the interaction between TAF6 and TAF9, suggesting that the formation of the complex between these two TFIID subunits do not only depend on their histone fold motifs. In addition, the same mutants affect even more strongly the interaction between TAF6 and TAF9 in the context of a TAF5-TAF6-TAF9 complex. Expression of these mutants in HeLa cells reveals that most of them are unstable, suggesting their poor incorporation within endogenous TFIID. Taken together, our results suggest that the conserved additional domains in histone fold-containing subunits of TFIID and of co-activator SAGA are important for the assembly of these complexes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.