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Structural studies on subunits τ60/τ91 of yeast transcription factor IIIC (TFIIIC).

Abstract : TFIIIC is a DNA binding complex that serves as an assembly factor in class III genes. It is a multisubunit protein of about 600 kDa organized in two large domains, τA and τB, of similar size and mass. TFIIIC consists of six polypeptides τ138, τ131, τ95, τ91, τ60 and τ55. τ138, τ91 and τ60 make up the τB subcomplex and τ131, τ95 and τ55 belong to the τA subassembly. This work presents the X-ray crystal structure of yeast τ60 complexed with the C-terminal part of τ91 at 3.2 Å resolution. τ60 consists of a N-terminal β-propeller domain and a C-terminal domain that is an overall new fold and very likely is the part that links τA with τB and contacts the TBP. Δτ91 is also a β-propeller. The interacting region between the two proteins involves residues in the two β-propellers, whereas the C-terminal domain of τ60 does not contribute at all to the interaction. This novel β-propeller – β-propeller interaction appears to be of great importance for the formation of a very stable τB complex able to bind with high affinity and stability to the B box. Our results provide a starting point for further structural and functional studies aimed at elucidating the mechanism of preinitiation complex formation in the RNA polymerase III transcription machinery.
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Contributor : Anastasia Mylona <>
Submitted on : Friday, January 27, 2006 - 10:23:00 AM
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  • HAL Id : tel-00011478, version 1




Anastasia Mylona. Structural studies on subunits τ60/τ91 of yeast transcription factor IIIC (TFIIIC).. Biomolecules [q-bio.BM]. Université Joseph-Fourier - Grenoble I, 2005. English. ⟨tel-00011478⟩



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