Structural basis for RNA polymerase III transcription repression by Maf1

Matthias K. Vorländer, Florence Baudin, Robyn D. Moir, René Wetzel, Wim J.H. Hagen, Ian M. Willis, Christoph W. Müller

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)229-232
Number of pages4
JournalNature Structural and Molecular Biology
Volume27
Issue number3
DOIs
StatePublished - Mar 1 2020

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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