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Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
Published on: August 17, 2022
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The complete structure of the human TFIIH core complex
Basil J Greber1,2, Daniel B Toso1, Jie Fang3
1California Institute for Quantitative Biosciences, University of California, Berkeley, United States.
Elife
|March 13, 2019
Summary
We determined the complete structure of the human Transcription factor IIH (TFIIH) core complex. This reveals how TFIIH assembles and how disease mutations impact its function in DNA repair and transcription.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Transcription factor IIH (TFIIH) is essential for RNA polymerase II transcription initiation and DNA repair.
- The TFIIH core complex contains XPB and XPD ATPase/helicase subunits implicated in human diseases.
- Previous structural studies offered limited insight into TFIIH architecture and its role in transcription complexes.
Purpose of the Study:
- To determine the complete structure of the human TFIIH core complex.
- To elucidate the molecular mechanisms underlying TFIIH assembly and function.
- To map disease-associated mutations within the TFIIH structure.
Main Methods:
- Phase-plate cryo-electron microscopy (cryo-EM) at 3.7 Å resolution.
- Structural determination of the human TFIIH core complex.
Main Results:
- The complete structure of the human TFIIH core complex was resolved.
- Revealed the molecular basis of TFIIH assembly, including XPB recruitment by p52.
- Identified a potential regulatory role for p62 in XPD function and mapped disease mutations.
Conclusions:
- The determined structure provides a comprehensive view of the TFIIH core complex.
- Offers insights into TFIIH's role in DNA repair and transcription initiation.
- Facilitates understanding of TFIIH-related human diseases and potential therapeutic strategies.
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