Subunit architecture of general transcription factor TFIIH
Subunit architecture of general transcription factor TFIIH
Structures of complete 10-subunit yeast TFIIH and of a nested set of subcomplexes, containing 5, 6, and 7 subunits, have been determined by electron microscopy (EM) and 3D reconstruction. Consistency among all the structures establishes the location of the “minimal core” subunits (Ssl1, Tfb1, Tfb2, Tfb4, and Tfb5), and additional densities can be specifically attributed to Rad3, Ssl2, and the TFIIK trimer. These results can be further interpreted by placement of previous X-ray structures into the additional densities to give a preliminary picture of the RNA polymerase II preinitiation complex. In this picture, the key catalytic components of TFIIH, the Ssl2 ATPase/helicase and the Kin28 protein kinase are in proximity to their targets, downstream promoter DNA and the RNA polymerase C-terminal domain.
- Scripps Research Institute United States
- Roosevelt University United States
- Massachusetts Institute of Technology United States
- Stanford University United States
Models, Molecular, Protein Subunits, Calmodulin, Staining and Labeling, Multiprotein Complexes, Electrophoresis, Polyacrylamide Gel, Saccharomyces cerevisiae, Transcription Factor TFIIH
Models, Molecular, Protein Subunits, Calmodulin, Staining and Labeling, Multiprotein Complexes, Electrophoresis, Polyacrylamide Gel, Saccharomyces cerevisiae, Transcription Factor TFIIH
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