Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor.
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Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor. / Penney, Mary; Samejima, Itaru; Wilkinson, Caroline; McInerny, Christopher; Mathiassen, Søs; Wallace, Mairi; Toda, Takashi; Hartmann-Petersen, Rasmus; Gordon, Colin.
In: P L o S One, Vol. 7, No. 11, 2012.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor.
AU - Penney, Mary
AU - Samejima, Itaru
AU - Wilkinson, Caroline
AU - McInerny, Christopher
AU - Mathiassen, Søs
AU - Wallace, Mairi
AU - Toda, Takashi
AU - Hartmann-Petersen, Rasmus
AU - Gordon, Colin
N1 - Artikel ID: e50796
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
U2 - 10.1371/journal.pone.0050796
DO - 10.1371/journal.pone.0050796
M3 - Journal article
C2 - 23209828
VL - 7
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 11
ER -
ID: 42014886