Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor.

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Documents

  • Mary Penney
  • Itaru Samejima
  • Caroline Wilkinson
  • Christopher McInerny
  • Søs Mathiassen
  • Mairi Wallace
  • Takashi Toda
  • Hartmann-Petersen, Rasmus
  • Colin Gordon
Here we report the result of a genetic screen for mutants resistant to the microtubule poison methyl benzimidazol-2-yl carbamate (MBC) that were also temperature sensitive for growth. In total the isolated mutants were distributed in ten complementation groups. Cloning experiments revealed that most of the mutants were in essential genes encoding various 26S proteasome subunits. We found that the proteasome mutants are multi-drug resistant due to stabilization of the stress-activated transcription factor Pap1. We show that the ubiquitylation and ultimately the degradation of Pap1 depend on the Rhp6/Ubc2 E2 ubiquitin conjugating enzyme and the Ubr1 E3 ubiquitin-protein ligase. Accordingly, mutants lacking Rhp6 or Ubr1 display drug-resistant phenotypes.
Original languageEnglish
JournalP L o S One
Volume7
Issue number11
Number of pages8
ISSN1932-6203
DOIs
Publication statusPublished - 2012

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