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PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression

Maf1 is the ‘master’ repressor of RNA polymerase III (Pol III) transcription in yeast, and is conserved in eukaryotes. Maf1 is a phospho-integrator, with unfavourable growth conditions leading to rapid Maf1 dephosphorylation, nuclear accumulation, binding to RNA Pol III at Pol III genes and transcri...

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Autores principales: Oler, Andrew J, Cairns, Bradley R
Formato: Online Artículo Texto
Lenguaje:English
Publicado: European Molecular Biology Organization 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3321174/
https://www.ncbi.nlm.nih.gov/pubmed/22333918
http://dx.doi.org/10.1038/emboj.2011.501
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author Oler, Andrew J
Cairns, Bradley R
author_facet Oler, Andrew J
Cairns, Bradley R
author_sort Oler, Andrew J
collection PubMed
description Maf1 is the ‘master’ repressor of RNA polymerase III (Pol III) transcription in yeast, and is conserved in eukaryotes. Maf1 is a phospho-integrator, with unfavourable growth conditions leading to rapid Maf1 dephosphorylation, nuclear accumulation, binding to RNA Pol III at Pol III genes and transcriptional repression. Here, we establish the protein phosphatase 4 (PP4) complex as the main Maf1 phosphatase, and define the involved catalytic (Pph3), scaffold (Psy2) and regulatory subunits (Rrd1, Tip41), as well as uninvolved subunits (Psy4, Rrd2). Multiple approaches support a central role for PP4 in Maf1 dephosphorylation, Maf1 nuclear localization and the rapid repression of Pol III in the nucleus. PP4 action is likely direct, as a portion of PP4 co-precipitates with Maf1, and purified PP4 dephosphorylates Maf1 in vitro. Furthermore, Pph3 mediates (either largely or fully) rapid Maf1 dephosphorylation in response to diverse stresses, suggesting PP4 plays a key role in the integration of cell nutrition and stress conditions by Maf1 to enable Pol III regulation.
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spelling pubmed-33211742012-04-09 PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression Oler, Andrew J Cairns, Bradley R EMBO J Article Maf1 is the ‘master’ repressor of RNA polymerase III (Pol III) transcription in yeast, and is conserved in eukaryotes. Maf1 is a phospho-integrator, with unfavourable growth conditions leading to rapid Maf1 dephosphorylation, nuclear accumulation, binding to RNA Pol III at Pol III genes and transcriptional repression. Here, we establish the protein phosphatase 4 (PP4) complex as the main Maf1 phosphatase, and define the involved catalytic (Pph3), scaffold (Psy2) and regulatory subunits (Rrd1, Tip41), as well as uninvolved subunits (Psy4, Rrd2). Multiple approaches support a central role for PP4 in Maf1 dephosphorylation, Maf1 nuclear localization and the rapid repression of Pol III in the nucleus. PP4 action is likely direct, as a portion of PP4 co-precipitates with Maf1, and purified PP4 dephosphorylates Maf1 in vitro. Furthermore, Pph3 mediates (either largely or fully) rapid Maf1 dephosphorylation in response to diverse stresses, suggesting PP4 plays a key role in the integration of cell nutrition and stress conditions by Maf1 to enable Pol III regulation. European Molecular Biology Organization 2012-03-21 2012-02-14 /pmc/articles/PMC3321174/ /pubmed/22333918 http://dx.doi.org/10.1038/emboj.2011.501 Text en Copyright © 2012, European Molecular Biology Organization https://creativecommons.org/licenses/by-nc-sa/3.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Noncommercial Share Alike 3.0 Unported License, which allows readers to alter, transform, or build upon the article and then distribute the resulting work under the same or similar license to this one. The work must be attributed back to the original author and commercial use is not permitted without specific permission.
spellingShingle Article
Oler, Andrew J
Cairns, Bradley R
PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title_full PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title_fullStr PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title_full_unstemmed PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title_short PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression
title_sort pp4 dephosphorylates maf1 to couple multiple stress conditions to rna polymerase iii repression
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3321174/
https://www.ncbi.nlm.nih.gov/pubmed/22333918
http://dx.doi.org/10.1038/emboj.2011.501
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