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

doi:10.1038/s41594-020-0383-y

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 journal › Article › peer-review

34 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 language	English (US)
Pages (from-to)	229-232
Number of pages	4
Journal	Nature Structural and Molecular Biology
Volume	27
Issue number	3
DOIs	https://doi.org/10.1038/s41594-020-0383-y
State	Published - Mar 1 2020

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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title = "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-{\AA}-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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AU - Vorländer, Matthias K.

AU - Baudin, Florence

AU - Moir, Robyn D.

AU - Wetzel, René

AU - Hagen, Wim J.H.

AU - Willis, Ian M.

AU - Müller, Christoph W.

PY - 2020/3/1

Y1 - 2020/3/1

N2 - 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.

AB - 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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JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

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Structural basis for RNA polymerase III transcription repression by Maf1

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