Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.

Avinash B Patel, Basil J Greber, Eva Nogales

Journal: Current opinion in structural biology 2021;61():17-24

PMID: 31751889

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Abstract

TFIID is a large multiprotein assembly that serves as a general transcription factor for transcription initiation by eukaryotic RNA polymerase II (Pol II). TFIID is involved in the recognition of the core promoter sequences and neighboring chromatin marks, and can interact with gene-specific activators and repressors. In order to obtain a better molecular and mechanistic understanding of the function of TFIID, its structure has been pursued for many years. However, the scarcity of TFIID and its highly flexible nature have made this pursuit very challenging. Recent breakthroughs, largely due to methodological advances in cryo-electron microscopy, have finally described the structure of this complex, both alone and engaged with core promoter DNA, revealing the functional significance of its conformational complexity in the process of core promoter recognition and initiation of Pol II transcription. Here, we review these recent structural insights and discuss their implications for our understanding of eukaryotic transcription initiation.

Address: Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Electronic address: [email protected].; Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA.; Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Electronic address: [email protected].

DOI: 10.1016/j.sbi.2019.10.001

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MeSH Terms: Amino Acid Sequence, Fungal Proteins, Humans, Molecular Conformation, Molecular Docking Simulation, Molecular Dynamics Simulation, Promoter Regions, Genetic, Protein Binding, Protein Conformation, Structure-Activity Relationship, TATA-Box Binding Protein, Transcription Factor TFIID