Structure of the τ60/Δτ91 Subcomplex of Yeast Transcription Factor IIIC: Insights into Preinitiation Complex Assembly
| Autor: | Christoph W. Müller, Carlos Fernández-Tornero, Pierre Legrand, Anastasia Mylona, Melina Haupt, Joël Acker, André Sentenac |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Folding Transcription Genetic Protein Conformation TATA box Molecular Sequence Data macromolecular substances Crystallography X-Ray RNA polymerase III Protein Structure Secondary Transcription Factors TFIII Humans Amino Acid Sequence Molecular Biology biology Promoter Cell Biology Molecular biology Recombinant Proteins Cell biology Protein Structure Tertiary Transcription preinitiation complex biology.protein Transcription factor II E TATA-binding protein Transcription factor II D Dimerization Transcription factor II A Protein Binding |
| Zdroj: | Molecular Cell. 24(2):221-232 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2006.08.013 |
| Popis: | Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the 3.2 A crystal structure of tau60 bound to a large C-terminal fragment of tau91 (Deltatau91). Deltatau91 protein contains a seven-bladed propeller preceded by an N-terminal extension, whereas tau60 contains a structurally homologous propeller followed by a C-terminal domain with a novel alpha/beta fold. The two propeller domains do not have any detectable DNA binding activity and mediate heterodimer formation that may serve as scaffold for tau138 assembly. We show that the C-terminal tau60 domain interacts with the TATA binding protein (TBP). Recombinant tauB recruits TBP and stimulates TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a combined contribution of tauA and tauB to preinitiation complex formation. |
| Databáze: | OpenAIRE |
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