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Accueil > Départements > Biologie des Génomes > Stéphane CHEDIN & Laurent KURAS : Physiologie et Pathogénicité des Stress

Publications

2017


  • A. F. Amorim, D. Pinto, L. Kuras, et L. Fernandes, « Absence of Gim proteins, but not GimC complex, alter stress-induced transcription », Biochimica Et Biophysica Acta, 2017.
    Résumé : Saccharomyces cerevisiae GimC (mammalian Prefoldin) is a hexameric (Gim1-6) cytoplasmic complex involved in the folding pathway of actin/tubulin. In contrast to a shared role in GimC complex, we show that absence of individual Gim proteins results in distinct stress responses. No concomitant alteration in F-actin integrity was observed. Transcription of stress responsive genes is altered in gim2Δ, gim3Δ and gim6Δ mutants: TRX2 gene is induced in these mutants but with a profile diverging from type cells, whereas CTT1 and HSP26 fail to be induced. Remaining gimΔ mutants display stress transcript abundance comparable to wild type cells. No alteration in the nuclear localization of the transcriptional activators for TRX2 (Yap1) and CTT1/HSP26 (Msn2) was observed in gim2Δ. In accordance with TRX2 induction, RNA polymerase II occupancy at TRX2 discriminates the wild type from gim2Δ and gim6Δ. In contrast, RNA polymerase II occupancy at CTT1 is similar in wild type and gim2Δ, but higher in gim6Δ. The absence of active RNA polymerase II at CTT1 in gim2Δ, but not in wild type and gim1Δ, explains the respective CTT1 transcript outputs. Altogether our results put forward the need of Gim2, Gim3 and Gim6 in oxidative and osmotic stress activated transcription; others Gim proteins are dispensable. Consequently, the participation of Gim proteins in activated-transcription is independent from the GimC complex.
    Mots-clés : DBG, Gim proteins, PEPS, stress, Transcription regulation.


  • C. Voisset, M. Blondel, G. W. Jones, G. Friocourt, G. Stahl, S. Chédin, V. Beringue, et R. Gillet, « The double life of the ribosome: when its protein folding activity supports prion propagation », Prion, p. 00-00, mars 2017.

2016

2015



  • A. Kaya, M. V. Gerashchenko, I. Seim, J. Labarre, M. B. Toledano, et V. N. Gladyshev, « Adaptive aneuploidy protects against thiol peroxidase deficiency by increasing respiration via key mitochondrial proteins », Proceedings of the National Academy of Sciences, vol. 112, nᵒ 34, p. 10685-10690, août 2015.
    Mots-clés : Adaptation, Physiological, Aneuploidy, Antimycin A, BIOCELL, Ahromnsgme Deletion, Chromosomes, Fungal, Cytochrome-c Peroxidase, DBG, Electron Transport, Gene Deletion, Gene Dosage, Genes, Fungal, Heat-Shock Proteins, Hydrogen Peroxide, Membrane Proteins, Mitochondrial Proteins, Oligomycins, oxidative stress, Oxidoreductases Acting on Sulfur Group Donors, PEPS, Peroxidases, Reactive Oxygen Species, respiration, Rotenone, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, SOC, thiol peroxidase.
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Publications des membres de l’équipe avant 2015

-  Hatem E, Berthonaud V, Dardalhon M, et al. Glutathione is essential to preserve nuclear function and cell survival under oxidative stress. Free Radic Biol Med. 2014 ;67:103–14. doi:10.1016/j.freeradbiomed.2013.10.807.

- Devineau S, Boulard Y, Labarre J. Protéines et nanoparticules, ça colle... ou pas. Biofutur. 2013 ;347:34–38.

-  Lacombe T, Poh SL, Barbey R, Kuras L. Mediator is an intrinsic component of the basal RNA polymerase II machinery in vivo. Nucleic Acids Res. 2013 ;41(21):9651–62. doi:10.1093/nar/gkt701.

-  Mathé C, Devineau S, Aude J-C, et al. Structural determinants for protein adsorption/non-adsorption to silica surface. PLoS One. 2013 ;8(11):e81346. doi:10.1371/journal.pone.0081346.

-  Zhou L, Le Roux G, Ducrot C, et al. Repression of class I transcription by cadmium is mediated by the protein phosphatase 2A. Nucleic Acids Res. 2013 ;41(12):6087–97. doi:10.1093/nar/gkt335.

-  Baudouin-Cornu P, Lagniel G, Kumar C, Huang M-E, Labarre J. Glutathione degradation is a key determinant of glutathione homeostasis. J Biol Chem. 2012 ;287(7):4552–61. doi:10.1074/jbc.M111.315705.

-  Peric D, Labarre J, Chevalier F, Rousselet G. Impairing the microRNA biogenesis pathway induces proteome modifications characterized by size bias and enrichment in antioxidant proteins. Proteomics. 2012 ;12(14):2295–302. doi:10.1002/pmic.201100461.

-  Molin M, Yang J, Hanzén S, Toledano MB, Labarre J, Nyström T. Life span extension and H(2)O(2) resistance elicited by caloric restriction require the peroxiredoxin Tsa1 in Saccharomyces cerevisiae. Mol Cell. 2011 ;43(5):823–33. doi:10.1016/j.molcel.2011.07.027.

-  Cormier L, Barbey R, Kuras L. Transcriptional plasticity through differential assembly of a multiprotein activation complex. Nucleic Acids Res. 2010 ;38(15):4998–5014. doi:10.1093/nar/gkq257.

-  Delalande O, Desvaux H, Godat E, et al. Cadmium-glutathione solution structures provide new insights into heavy metal detoxification. FEBS J. 2010 ;277(24):5086–96. doi:10.1111/j.1742-4658.2010.07913.x.

-  Gardarin A, Chédin S, Lagniel G, et al. Endoplasmic reticulum is a major target of cadmium toxicity in yeast. Mol Microbiol. 2010 ;76(4):1034–48. doi:10.1111/j.1365-2958.2010.07166.x.

-  Godat E, Madalinski G, Muller L, Heilier J-F, Labarre J, Junot C. Mass spectrometry-based methods for the determination of sulfur and related metabolite concentrations in cell extracts. Methods Enzymol. 2010 ;473:41–76. doi:10.1016/S0076-6879(10)73002-0.

-  Baudouin-Cornu P, Lagniel G, Chédin S, Labarre J. Development of a new method for absolute protein quantification on 2-D gels. Proteomics. 2009 ;9(20):4606–15. doi:10.1002/pmic.200800975.

-  Boisnard S, Lagniel G, Garmendia-Torres C, et al. H2O2 activates the nuclear localization of Msn2 and Maf1 through thioredoxins in Saccharomyces cerevisiae. Eukaryot Cell. 2009 ;8(9):1429–38. doi:10.1128/EC.00106-09.

-  Labarre J, Forestier C, Bourguignon J. Mécanismes de détoxication du cadmium chez les eucaryotes. In : Ménager M-T, Garnier-Laplace J, Goyffon M, eds. Toxicologie Nucléaire Environnementale et Humaine,. Lavoisier ; 2009:213–229.

-  Baudouin-Cornu P. [Stoichiometric, my dear Watson !]. Med Sci (Paris). 2008 ;24(5):483–9.

-  Labarre J, Forestier C. Le cadmium : des mécanismes à élucider. Biofutur. 2008 ;291:30–33.

-  Madalinski G, Godat E, Alves S, et al. Direct introduction of biological samples into a LTQ-Orbitrap hybrid mass spectrometer as a tool for fast metabolome analysis. Anal Chem. 2008 ;80(9):3291–303. doi:10.1021/ac7024915.

-  Pereira Y, Lagniel G, Godat E, Baudouin-Cornu P, Junot C, Labarre J. Chromate causes sulfur starvation in yeast. Toxicol Sci. 2008 ;106(2):400–12. doi:10.1093/toxsci/kfn193.

-  Tribouillard-Tanvier D, Dos Reis S, Gug F, et al. Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs. PLoS One. 2008 ;3(5):e2174. doi:10.1371/journal.pone.0002174.

-  Alic N, Ayoub N, Landrieux E, et al. Selectivity and proofreading both contribute significantly to the fidelity of RNA polymerase III transcription. Proc Natl Acad Sci U S A. 2007 ;104(25):10400–5. doi:10.1073/pnas.0704116104.

-  Baudouin-Cornu P, Thomas D. Evolutionary biology : oxygen at life’s boundaries. Nature. 2007 ;445(7123):35–6. doi:10.1038/nature05521.

-  Baudouin-Cornu P, Thomas D. [On the role played by oxygen in evolution]. Med Sci (Paris). 2007 ;23(3):255–7.

-  Chédin S, Laferté A, Hoang T, Lafontaine DLJ, Riva M, Carles C. Is ribosome synthesis controlled by pol I transcription ? Cell Cycle. 2007 ;6(1):11–5.

-  Molin M, Renault J-P, Lagniel G, Pin S, Toledano M, Labarre J. Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast. Free Radic Biol Med. 2007 ;43(1):136–44. doi:10.1016/j.freeradbiomed.2007.04.007.

-  Thorsen M, Lagniel G, Kristiansson E, et al. Quantitative transcriptome, proteome, and sulfur metabolite profiling of the Saccharomyces cerevisiae response to arsenite. Physiol Genomics. 2007 ;30(1):35–43. doi:10.1152/physiolgenomics.00236.2006.

-  Baudouin-Cornu P, Labarre J. Regulation of the cadmium stress response through SCF-like ubiquitin ligases : comparison between Saccharomyces cerevisiae, Schizosaccharomyces pombe and mammalian cells. Biochimie. 2006 ;88(11):1673–85. doi:10.1016/j.biochi.2006.03.001.

-  Bragg JG, Thomas D, Baudouin-Cornu P. Variation among species in proteomic sulphur content is related to environmental conditions. Proc Biol Sci. 2006 ;273(1591):1293–300. doi:10.1098/rspb.2005.3441.

-  Laferté A, Favry E, Sentenac A, Riva M, Carles C, Chédin S. The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components. Genes Dev. 2006 ;20(15):2030–40. doi:10.1101/gad.386106.

-  Leroy C, Cormier L, Kuras L. Independent recruitment of mediator and SAGA by the activator Met4. Mol Cell Biol. 2006 ;26(8):3149–63. doi:10.1128/MCB.26.8.3149-3163.2006.

-  Menant A, Baudouin-Cornu P, Peyraud C, Tyers M, Thomas D. Determinants of the ubiquitin-mediated degradation of the Met4 transcription factor. J Biol Chem. 2006 ;281(17):11744–54. doi:10.1074/jbc.M600037200.

-  Tamás MJ, Labarre J, Toledano MB, Wysocki R. Mechanisms of toxic metal tolerance in yeast. In : ; 2006:395–454. doi:10.1007/4735_105.

-  Barbey R, Baudouin-Cornu P, Lee TA, et al. Inducible dissociation of SCF(Met30) ubiquitin ligase mediates a rapid transcriptional response to cadmium. EMBO J. 2005 ;24(3):521–32. doi:10.1038/sj.emboj.7600556.

-  ELafaye A, Junot C, Pereira Y, et al. Combined proteome and metabolite-profiling analyses reveal surprising insights into yeast sulfur metabolism. J Biol Chem. 2005 ;280(26):24723–30. doi:10.1074/jbc.M502285200.

-  Baudouin-Cornu P, Schuerer K, Marlière P, Thomas D. Intimate evolution of proteins. Proteome atomic content correlates with genome base composition. J Biol Chem. 2004 ;279(7):5421–8. doi:10.1074/jbc.M306415200.

-  Bourbon H-M, Aguilera A, Ansari AZ, et al. A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II. Mol Cell. 2004 ;14(5):553–7. doi:10.1016/j.molcel.2004.05.011.

-  Fiévet J, Dillmann C, Lagniel G, et al. Assessing factors for reliable quantitative proteomics based on two-dimensional gel electrophoresis. Proteomics. 2004 ;4(7):1939–49. doi:10.1002/pmic.200300731.

-  Kuras L. Characterization of protein-DNA association in vivo by chromatin immunoprecipitation. Methods Mol Biol. 2004 ;284:147–62. doi:10.1385/1-59259-816-1:147.

-  Biteau B, Labarre J, Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature. 2003 ;425(6961):980–4. doi:10.1038/nature02075.

-  Kuras L, Borggrefe T, Kornberg RD. Association of the Mediator complex with enhancers of active genes. Proc Natl Acad Sci U S A. 2003 ;100(24):13887–91. doi:10.1073/pnas.2036346100.

-  Fauchon M, Lagniel G, Aude J-C, et al. Sulfur Sparing in the Yeast Proteome in Response to Sulfur Demand. Mol Cell. 2002 ;9(4):713–723. doi:10.1016/S1097-2765(02)00500-2.

-  Geisberg J V., Moqtaderi Z, Kuras L, Struhl K. Mot1 Associates with Transcriptionally Active Promoters and Inhibits Association of NC2 in Saccharomyces cerevisiae. Mol Cell Biol. 2002 ;22(23):8122–8134. doi:10.1128/MCB.22.23.8122-8134.2002.

-  Kuras L, Rouillon A, Lee T a, Barbey R, Tyers M, Thomas D. Dual regulation of the met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment. Mol Cell. 2002 ;10(1):69–80.

-  Mencía M, Moqtaderi Z, Geisberg J V, Kuras L, Struhl K. Activator-specific recruitment of TFIID and regulation of ribosomal protein genes in yeast. Mol Cell. 2002 ;9(4):823–33.

-  Baudouin-Cornu P, Surdin-Kerjan Y, Marlière P, Thomas D. Molecular evolution of protein atomic composition. Science. 2001 ;293(5528):297–300. doi:10.1126/science.1061052.

-  Vido K, Spector D, Lagniel G, Lopez S, Toledano MB, Labarre J. A proteome analysis of the cadmium response in Saccharomyces cerevisiae. J Biol Chem. 2001 ;276(11):8469–74. doi:10.1074/jbc.M008708200.

-  Spector D, Labarre J, Toledano MB. A genetic investigation of the essential role of glutathione : mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast. J Biol Chem. 2001 ;276(10):7011–6. doi:10.1074/jbc.M009814200.

-  Kuras L, Kosa P, Mencia M, Struhl K. TAF-Containing and TAF-independent forms of transcriptionally active TBP in vivo. Science. 2000

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