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From Proteopedia
Taf14 ET domain in complex with C-terminal tail of Taf2
Structural highlights
FunctionTAF14_YEAST Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedThe assembly and function of the yeast general transcription factor TFIID complex requires specific contacts between its Taf14 and Taf2 subunits, however, the mechanism underlying these contacts remains unclear. Here, we determined the molecular and structural basis by which the YEATS and ET domains of Taf14 bind to the C-terminal tail of Taf2 and identified a unique DNA-binding activity of the linker region connecting the two domains. We show that in the absence of ligands the linker region of Taf14 is occluded by the surrounding domains, and therefore the DNA binding function of Taf14 is autoinhibited. Binding of Taf2 promotes a conformational rearrangement in Taf14, resulting in a release of the linker for the engagement with DNA and the nucleosome. Genetic in vivo data indicate that the association of Taf14 with both Taf2 and DNA is essential for transcriptional regulation. Our findings provide a basis for deciphering the role of individual TFIID subunits in mediating gene transcription. Taf2 mediates DNA binding of Taf14.,Klein BJ, Feigerle JT, Zhang J, Ebmeier CC, Fan L, Singh RK, Wang WW, Schmitt LR, Lee T, Hansen KC, Liu WR, Wang YX, Strahl BD, Anthony Weil P, Kutateladze TG Nat Commun. 2022 Jun 8;13(1):3177. doi: 10.1038/s41467-022-30937-w. PMID:35676274[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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