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TitleStructural basis for RNA polymerase III transcription repression by Maf1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 3, Page 229-232, Year 2020
Publish dateFeb 17, 2020
AuthorsMatthias K Vorländer / Florence Baudin / Robyn D Moir / René Wetzel / Wim J H Hagen / Ian M Willis / Christoph W Müller /
PubMed AbstractMaf1 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 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.
External linksNat Struct Mol Biol / PubMed:32066962 / PubMed Central
MethodsEM (single particle)
Resolution3.25 Å
Structure data

10595

6tut

EMDB-10595, PDB-6tut:
Cryo-EM structure of the RNA Polymerase III-Maf1 complex
Method: EM (single particle) / Resolution: 3.25 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsTRANSCRIPTION / RNA Polymerase III / Pol III / Maf1 / transcription inhibition

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