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

Avinash B Patel; Basil J Greber; Eva Nogales

doi:10.1016/j.sbi.2019.10.001

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

Curr Opin Struct Biol. 2020 Apr:61:17-24. doi: 10.1016/j.sbi.2019.10.001. Epub 2019 Nov 18.

Authors

Avinash B Patel¹, Basil J Greber², Eva Nogales³

Affiliations

¹ 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].
² 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.
³ 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].

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.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

Amino Acid Sequence
Fungal Proteins / chemistry
Fungal Proteins / metabolism
Humans
Molecular Conformation
Molecular Docking Simulation*
Molecular Dynamics Simulation*
Promoter Regions, Genetic*
Protein Binding
Protein Conformation*
Structure-Activity Relationship
TATA-Box Binding Protein / chemistry
TATA-Box Binding Protein / metabolism
Transcription Factor TFIID / chemistry*
Transcription Factor TFIID / metabolism

Substances

Fungal Proteins
TATA-Box Binding Protein
Transcription Factor TFIID

Abstract

Publication types

MeSH terms

Substances

Grants and funding