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Updated: Dec 28, 2025

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Structural basis for RNA polymerase III transcription repression by Maf1
Matthias K Vorländer1,2, Florence Baudin1, Robyn D Moir3
1Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Abstract:
Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes ranging from metabolic efficiency to lifespan. Here, we present a 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds the mobile C34 winged helix 2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the preinitiation complex.
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