Structural basis for RNA polymerase III transcription repression by Maf1

Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes from metabolic efficiency to lifespan. Here, we present a 3.3 Å cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds...

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Autores principales: Vorländer, Matthias K., Baudin, Florence, Moir, Robyn D., Wetzel, René, Hagen, Wim J. H., Willis, Ian M., Müller, Christoph W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104376/
https://www.ncbi.nlm.nih.gov/pubmed/32066962
http://dx.doi.org/10.1038/s41594-020-0383-y
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author Vorländer, Matthias K.
Baudin, Florence
Moir, Robyn D.
Wetzel, René
Hagen, Wim J. H.
Willis, Ian M.
Müller, Christoph W.
author_facet Vorländer, Matthias K.
Baudin, Florence
Moir, Robyn D.
Wetzel, René
Hagen, Wim J. H.
Willis, Ian M.
Müller, Christoph W.
author_sort Vorländer, Matthias K.
collection PubMed
description Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes from metabolic efficiency to lifespan. Here, we present a 3.3 Å 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 WH2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the pre-initiation complex.
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spelling pubmed-71043762020-08-17 Structural basis for RNA polymerase III transcription repression by Maf1 Vorländer, Matthias K. Baudin, Florence Moir, Robyn D. Wetzel, René Hagen, Wim J. H. Willis, Ian M. Müller, Christoph W. Nat Struct Mol Biol Article Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes from metabolic efficiency to lifespan. Here, we present a 3.3 Å 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 WH2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the pre-initiation complex. 2020-02-17 2020-03 /pmc/articles/PMC7104376/ /pubmed/32066962 http://dx.doi.org/10.1038/s41594-020-0383-y Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Vorländer, Matthias K.
Baudin, Florence
Moir, Robyn D.
Wetzel, René
Hagen, Wim J. H.
Willis, Ian M.
Müller, Christoph W.
Structural basis for RNA polymerase III transcription repression by Maf1
title Structural basis for RNA polymerase III transcription repression by Maf1
title_full Structural basis for RNA polymerase III transcription repression by Maf1
title_fullStr Structural basis for RNA polymerase III transcription repression by Maf1
title_full_unstemmed Structural basis for RNA polymerase III transcription repression by Maf1
title_short Structural basis for RNA polymerase III transcription repression by Maf1
title_sort structural basis for rna polymerase iii transcription repression by maf1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104376/
https://www.ncbi.nlm.nih.gov/pubmed/32066962
http://dx.doi.org/10.1038/s41594-020-0383-y
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