Year: 2022
Type: article
Abstract: The 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.
Source: Nature Communications
Institutions: University of Colorado Anschutz, Vanderbilt University, Stanford University, University of North Carolina at Chapel Hill, University of Colorado Boulder, University of Colorado System, Frederick National Laboratory for Cancer Research, National Cancer Institute, Texas A&M University, National Institutes of Health, Center for Cancer Research
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,890
Funders: U.S. Department of Energy, U.S. Department of Health and Human Services, Division of Cancer Prevention, National Cancer Institute, National Institutes of Health, Office of Science, National Institute on Aging, National Heart, Lung, and Blood Institute, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases, Argonne National Laboratory
Awards: G102163711, G1045712244, G107546177, G1313983767, Interdomain crosstalk in MORC3, G1505794299, G1664757510, Quadrupole-Orbitrap Mass Spectrometer, Epigenetic mechanisms for regulation of p300, G1994702215, G2101401529, G2287611682, G262962599, G2887060908, G3075337988, G3152346458, G3157186215, G3266081141, G340565428, G4055571200, Structure of RNA Polymerase II, G4508749629, G4735631139, G498139845, G5106849484, The role of JADE in HBO complexes, G5604825015, G5607048534, Targeting acetylated histone H4 by MLL4, G6453829601, G6848031779, G6918803902, G7087489534, Three-Dimensional Structure of Eukaryote Chromosomes, G7368700025, G7529774362, G7581645272, Develop General Methods for the Synthesis of Proteins with Posttranslational Lysine Modifications, G9000256503, Molecular analysis of ASH1L, Targeting acetylated histone H4 by MLL4, Mechanisms of chromatin and transcriptional regulation, G969889393, G993149817
OpenAlex ID: W4281669998