Recent insights into the structure of TFIID, its assembly, and its binding to core promoter. (April 2020)

• Record Type: Journal Article
• Authors: Patel, Avinash B; Greber, Basil J; Nogales, Eva
• Is Part Of: Current opinion in structural biology. Volume 61(2020)
• Page Start: 17
• Page End: 24
• Publication Date: 2020-04
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2019.10.001
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: TFIID is a general transcription factor for RNA polymerase II and functions in promoter recognition and deposition of TBP Cryo-EM has revealed the structure and dynamics of human TFIID and suggests a mechanism of TBP deposition onto DNA The cryo-EM structures of human and yeast TFIID are compared and their differences are discussed in a functional context The recent structural results suggest a model for the mechanism of TFIID assembly from sub-modules 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.