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

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Standard

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.

I: P L o S One, Bind 7, Nr. 11, 2012.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Penney, M, Samejima, I, Wilkinson, C, McInerny, C, Mathiassen, S, Wallace, M, Toda, T, Hartmann-Petersen, R & Gordon, C 2012, 'Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor.', P L o S One, bind 7, nr. 11. https://doi.org/10.1371/journal.pone.0050796

APA

Penney, M., Samejima, I., Wilkinson, C., McInerny, C., Mathiassen, S., Wallace, M., Toda, T., Hartmann-Petersen, R., & Gordon, C. (2012). Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor. P L o S One, 7(11). https://doi.org/10.1371/journal.pone.0050796

Vancouver

Penney M, Samejima I, Wilkinson C, McInerny C, Mathiassen S, Wallace M o.a. Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor. P L o S One. 2012;7(11). https://doi.org/10.1371/journal.pone.0050796

Author

Penney, Mary ; Samejima, Itaru ; Wilkinson, Caroline ; McInerny, Christopher ; Mathiassen, Søs ; Wallace, Mairi ; Toda, Takashi ; Hartmann-Petersen, Rasmus ; Gordon, Colin. / Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor. I: P L o S One. 2012 ; Bind 7, Nr. 11.

Bibtex

@article{c7a198eebbee4714ba5a1e0926d60c3b,
title = "Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1transcription factor.",
abstract = "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.",
author = "Mary Penney and Itaru Samejima and Caroline Wilkinson and Christopher McInerny and S{\o}s Mathiassen and Mairi Wallace and Takashi Toda and Rasmus Hartmann-Petersen and Colin Gordon",
note = "Artikel ID: e50796",
year = "2012",
doi = "10.1371/journal.pone.0050796",
language = "English",
volume = "7",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "11",

}

RIS

TY - JOUR

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