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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 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.

Pubmed ID: 22333918

Authors

  • Oler AJ
  • Cairns BR

Journal

The EMBO journal

Publication Data

March 21, 2012

Associated Grants

None

Mesh Terms

  • Cell Nucleus
  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • Peptidylprolyl Isomerase
  • Phosphoprotein Phosphatases
  • Phosphorylation
  • RNA Polymerase III
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Transcription, Genetic