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Structural basis for RNA polymerase III transcription repression by Maf1.


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.

SUBMITTER: Vorlander MK 

PROVIDER: S-EPMC7104376 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Structural basis for RNA polymerase III transcription repression by Maf1.

Vorländer Matthias K MK   Baudin Florence F   Moir Robyn D RD   Wetzel René R   Hagen Wim J H WJH   Willis Ian M IM   Müller Christoph W CW  

Nature structural & molecular biology 20200217 3


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. ...[more]

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