More pieces to the puzzle: recent structural insights into class II transcription initiation
| Autor: | Eaazhisai Kandiah, Kapil Gupta, Imre Berger, Simon Trowitzsch, Matthias Haffke |
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| Rok vydání: | 2014 |
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Molecular Transcriptional Activation Protein Conformation TATA box Biology 03 medical and health sciences 0302 clinical medicine Structural Biology Animals Humans Molecular Biology RNA polymerase II holoenzyme 030304 developmental biology Genetics 0303 health sciences Mediator Complex General transcription factor Cell biology TAF1 Transcription preinitiation complex RNA Polymerase II Transcription factor II E Transcription Factors General Transcription factor II B 030217 neurology & neurosurgery Transcription factor II A |
| Zdroj: | Current Opinion in Structural Biology; Vol 24 |
| ISSN: | 0959-440X |
| Popis: | Class II transcription initiation is a highly regulated process and requires the assembly of a pre-initiation complex (PIC) containing DNA template, RNA polymerase II (RNAPII), general transcription factors (GTFs) TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIH and Mediator. RNAPII, TFIID, TFIIH and Mediator are large multiprotein complexes, each containing 10 and more subunits. Altogether, the PIC is made up of about 60 polypeptides with a combined molecular weight of close to 4MDa. Recent structural studies of key PIC components have significantly advanced our understanding of transcription initiation. TFIID was shown to bind promoter DNA in a reorganized state. The architecture of a core-TFIID complex was elucidated. Crystal structures of the TATA-binding protein (TBP) bound to TBP-associated factor 1 (TAF1), RNAPII-TFIIB complexes and the Mediator head module were solved. The overall architectures of large PIC assemblies from human and yeast have been determined by electron microscopy (EM). Here we review these latest structural insights into the architecture and assembly of the PIC, which reveal exciting new mechanistic details of transcription initiation. |
| Databáze: | OpenAIRE |
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