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Structure of human TFIID and mechanism of TBP loading onto promoter DNA.

ABSTRACT: The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter.

SUBMITTER: Patel AB

PROVIDER: S-EPMC6446905 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Structure of human TFIID and mechanism of TBP loading onto promoter DNA.

Patel Avinash B AB Louder Robert K RK Greber Basil J BJ Grünberg Sebastian S Luo Jie J Fang Jie J Liu Yutong Y Ranish Jeff J Hahn Steve S Nogales Eva E

Science (New York, N.Y.) 20181115 6421

The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter ...[more]

PMID: 30442764

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