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

The EMBO Journal
Andrew J Oler, Bradley R Cairns

Abstract

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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Citations

Apr 20, 2013·Chemical Reviews·Argyris Papantonis, Peter R Cook
Aug 1, 2012·Immunology and Cell Biology·Diana S HansenTania F de-Koning Ward
Dec 4, 2012·Biochimica Et Biophysica Acta·Magdalena Boguta
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Apr 9, 2014·Proceedings of the National Academy of Sciences of the United States of America·Indra A ShaltielRené H Medema
Feb 4, 2014·FEMS Microbiology Reviews·Michaela ConradJohan M Thevelein
Nov 2, 2016·Molecular Microbiology·Gabriela Romero-MezaSantiago Martínez-Calvillo
Dec 3, 2016·Biochemical Society Transactions·Tomasz W Turowski, David Tollervey
Jul 13, 2021·Frontiers in Molecular Biosciences·Araceli González-JiménezOlga Calvo

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Methods Mentioned

BETA
immunoprecipitation
nuclear translocation
ChIP
co-IP
environmental stress

Software Mentioned

iCycler
ImageQuant

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