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    Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly

    Mylona, Anastasia and Fernandez-Tornero, C. and Legrand, P. and Haupt, M. and Sentenac, A. and Acker, J. and Müller, C.W. (2006) Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly. Molecular Cell 24 (2), pp. 221-232. ISSN 1097-2765.

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    Abstract

    Yeast RNA polymerase III is recruited upon binding of subcomplexes τA and τB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The τB subcomplex consists of subunits τ60, τ91, and τ138. We determined the 3.2 Å crystal structure of τ60 bound to a large C-terminal fragment of τ91 (Δτ91). Δτ91 protein contains a seven-bladed propeller preceded by an N-terminal extension, whereas τ60 contains a structurally homologous propeller followed by a C-terminal domain with a novel α/β fold. The two propeller domains do not have any detectable DNA binding activity and mediate heterodimer formation that may serve as scaffold for τ138 assembly. We show that the C-terminal τ60 domain interacts with the TATA binding protein (TBP). Recombinant τB recruits TBP and stimulates TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a combined contribution of τA and τB to preinitiation complex formation.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 07 May 2019 16:02
    Last Modified: 07 May 2019 16:02
    URI: http://eprints.bbk.ac.uk/id/eprint/27434

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