D. L. Hatfield, P. A. Tsuji, B. A. Carlson, and V. N. Gladyshev, Selenium and selenocysteine: roles in cancer, health, and development, Trends in Biochemical Sciences, vol.39, issue.3, pp.112-120, 2014.
DOI : 10.1016/j.tibs.2013.12.007
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3943681

D. L. Hatfield and V. N. Gladyshev, How Selenium Has Altered Our Understanding of the Genetic Code, Molecular and Cellular Biology, vol.22, issue.11, pp.3565-3576, 2002.
DOI : 10.1128/MCB.22.11.3565-3576.2002

S. Misra, M. Boylan, A. Selvam, J. E. Spallholz, and M. Bjornstedt, Redox-Active Selenium Compounds???From Toxicity and Cell Death to Cancer Treatment, Nutrients, vol.11, issue.5, pp.3536-3556, 2015.
DOI : 10.3390/ijms13089649
URL : http://doi.org/10.3390/nu7053536

L. Flohe, W. A. Gunzler, and H. H. Schock, Glutathione peroxidase: A selenoenzyme, FEBS Letters, vol.49, issue.1, pp.132-134, 1973.
DOI : 10.1016/0014-5793(73)80755-0

M. P. Rayman, Selenium in cancer prevention: a review of the evidence and mechanism of action, Proceedings of the Nutrition Society, vol.61, issue.04, pp.527-542, 2005.
DOI : 10.1207/s15327914nc4902_9

M. P. Rayman, Selenium and human health, The Lancet, vol.379, issue.9822, pp.1256-1268, 2012.
DOI : 10.1016/S0140-6736(11)61452-9

A. J. Duffield-lillico, Selenium Supplementation and Secondary Prevention of Nonmelanoma Skin Cancer in a Randomized Trial, CancerSpectrum Knowledge Environment, vol.95, issue.19, pp.1477-1481, 2003.
DOI : 10.1093/jnci/djg061

S. Stranges, Effects of Long-Term Selenium Supplementation on the Incidence of Type 2 Diabetes, Annals of Internal Medicine, vol.147, issue.4, pp.217-223, 2007.
DOI : 10.7326/0003-4819-147-4-200708210-00175

S. M. Lippman, Effect of Selenium and Vitamin E on Risk of Prostate Cancer and Other Cancers, JAMA, vol.301, issue.1, pp.39-51, 2009.
DOI : 10.1001/jama.2008.864

C. M. Weekley and H. H. Harris, Which form is that? The importance of selenium speciation and metabolism in the prevention and treatment of disease, Chemical Society Reviews, vol.33, issue.Pt 1, pp.8870-8894, 2013.
DOI : 10.1093/jnci/djt186

M. Zorn, C. H. Ihling, R. Golbik, R. G. Sawers, and A. Sinz, Selective selC-Independent Selenocysteine Incorporation into Formate Dehydrogenases, PLoS ONE, vol.331, issue.4, p.61913, 2013.
DOI : 10.1371/journal.pone.0061913.s001
URL : http://doi.org/10.1371/journal.pone.0061913

K. Bierla, A comparative study of the Se/S substitution in methionine and cysteine in Se-enriched yeast using an inductively coupled plasma mass spectrometry (ICP MS)-assisted proteomics approach, Journal of Proteomics, vol.87, pp.26-39, 2013.
DOI : 10.1016/j.jprot.2013.05.010
URL : https://hal.archives-ouvertes.fr/hal-01505940

M. I. Jackson, G. F. Combs, and . Jr, 44761 | DOI: 10.1038/srep44761 13 Selenium and anticarcinogenesis: underlying mechanisms, Curr. Opin. Clin. Nutr. Metab. Care, vol.7, issue.11, pp.718-726, 2008.

L. Letavayova, V. Vlckova, and J. Brozmanova, Selenium: From cancer prevention to DNA damage, Toxicology, vol.227, issue.1-2, pp.1-14, 2006.
DOI : 10.1016/j.tox.2006.07.017

G. Peyroche, Sodium Selenide Toxicity Is Mediated by O2-Dependent DNA Breaks, PLoS ONE, vol.320, issue.5, p.36343, 2012.
DOI : 10.1371/journal.pone.0036343.s007
URL : https://hal.archives-ouvertes.fr/hal-00764441

E. Seitomer, B. Balar, D. He, P. R. Copeland, and T. G. Kinzy, oxidative stress pathways in growth inhibition by selenium, Molecular Nutrition & Food Research, vol.155, issue.11, pp.1305-1315, 2008.
DOI : 10.1002/mnfr.200700347

D. Manikova, Selenium Toxicity toward Yeast as Assessed by Microarray Analysis and Deletion Mutant Library Screen: A Role for DNA Repair, Chemical Research in Toxicology, vol.25, issue.8, pp.1598-1608, 2012.
DOI : 10.1021/tx300061n

J. Bockhorn, Genome-wide screen of Saccharomyces cerevisiae null allele strains identifies genes involved in selenomethionine resistance, Proc. Natl. Acad. Sci. USA 105, pp.17682-17687, 2008.
DOI : 10.1023/A:1009221810760

M. Lazard, M. Dauplais, S. Blanquet, and P. Plateau, *, Journal of Biological Chemistry, vol.290, issue.17, pp.10741-10750, 2015.
DOI : 10.1074/jbc.M115.640375

A. L. Schuh and A. Audhya, The ESCRT machinery: From the plasma membrane to endosomes and back again, Critical Reviews in Biochemistry and Molecular Biology, vol.17, issue.3, pp.242-261, 2014.
DOI : 10.1016/S1097-2765(00)00143-X

I. E. Vainberg, Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin, Cell, vol.93, issue.5, pp.863-873, 1998.
DOI : 10.1016/S0092-8674(00)81446-4
URL : http://doi.org/10.1016/s0092-8674(00)81446-4

M. G. Malkowski, Blocking S-adenosylmethionine synthesis in yeast allows selenomethionine incorporation and multiwavelength anomalous dispersion phasing, Proc. Natl. Acad. Sci. USA, pp.6678-6683, 2007.
DOI : 10.1107/S0907444996012255
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1850019

T. Kitajima, Y. Chiba, and Y. Jigami, Mutation of High-Affinity Methionine Permease Contributes to Selenomethionyl Protein Production in Saccharomyces cerevisiae, Applied and Environmental Microbiology, vol.76, issue.19, pp.6351-6359, 2010.
DOI : 10.1128/AEM.01026-10

J. R. Glover, S. Lindquist, and . Hsp104, Hsp104, Hsp70, and Hsp40, Cell, vol.94, issue.1, pp.73-82, 1998.
DOI : 10.1016/S0092-8674(00)81223-4
URL : http://doi.org/10.1016/s0092-8674(00)81223-4

K. K. Steffen, Ribosome Deficiency Protects Against ER Stress in Saccharomyces cerevisiae, Genetics, vol.191, issue.1, pp.107-118, 2012.
DOI : 10.1534/genetics.111.136549
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338253

S. C. Dos-santos, M. C. Teixeira, T. R. Cabrito, and I. Sa-correia, Yeast toxicogenomics: genome-wide responses to chemical stresses with impact in environmental health, pharmacology, and biotechnology, Frontiers in Genetics, vol.3, p.63, 2012.
DOI : 10.3389/fgene.2012.00063

S. C. Dos-santos and I. Sa-correia, Yeast toxicogenomics: lessons from a eukaryotic cell model and cell factory, Current Opinion in Biotechnology, vol.33, pp.183-191, 2015.
DOI : 10.1016/j.copbio.2015.03.001

G. Giaever, Functional profiling of the Saccharomyces cerevisiae genome, Nature, vol.57, issue.6896, pp.387-391, 2002.
DOI : 10.1073/pnas.95.25.14863

D. Hoepfner, High-resolution chemical dissection of a model eukaryote reveals targets, pathways and gene functions, Microbiological Research, vol.169, issue.2-3, pp.107-120, 2014.
DOI : 10.1016/j.micres.2013.11.004

F. Iorio, Discovery of drug mode of action and drug repositioning from transcriptional responses, Proc. Natl. Acad. Sci. USA, pp.14621-14626, 2010.
DOI : 10.1124/mol.106.030015

A. Y. Lee, Mapping the Cellular Response to Small Molecules Using Chemogenomic Fitness Signatures, Science, vol.263, issue.34, pp.208-211, 2014.
DOI : 10.1371/journal.ppat.1000939

R. Wysocki and M. J. Tamas, copes with toxic metals and metalloids, FEMS Microbiology Reviews, vol.34, issue.6, pp.925-951, 2010.
DOI : 10.1111/j.1574-6976.2010.00217.x

M. J. Tamas, S. K. Sharma, S. Ibstedt, T. Jacobson, and P. Christen, Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation, Biomolecules, vol.248, issue.1, pp.252-267, 2014.
DOI : 10.1159/000324514

S. Holland, Application of the comprehensive set of heterozygous yeast deletion mutants to elucidate the molecular basis of cellular chromium toxicity, Genome Biology, vol.8, issue.12, p.268, 2007.
DOI : 10.1186/gb-2007-8-12-r268

S. L. Holland, E. Ghosh, and S. V. Avery, Chromate-induced sulfur starvation and mRNA mistranslation in yeast are linked in a common mechanism of Cr toxicity, Toxicology in Vitro, vol.24, issue.6, pp.1764-1767, 2010.
DOI : 10.1016/j.tiv.2010.07.006

J. Navarro-yepes, Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways, Molecular Neurobiology, vol.557, issue.1, pp.5229-5251, 2016.
DOI : 10.1016/j.gene.2014.11.051

S. M. Roe, Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin, Journal of Medicinal Chemistry, vol.42, issue.2, pp.260-266, 1999.
DOI : 10.1021/jm980403y

K. J. Travers, Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation, Cell, vol.101, issue.3, pp.249-258, 2000.
DOI : 10.1016/S0092-8674(00)80835-1
URL : http://doi.org/10.1016/s0092-8674(00)80835-1

M. Y. Sherman and S. B. Qian, Less is more: improving proteostasis by translation slow down, Trends in Biochemical Sciences, vol.38, issue.12, pp.585-591, 2013.
DOI : 10.1016/j.tibs.2013.09.003

L. Ouerdane and Z. Mester, Production and Characterization of Fully Selenomethionine-Labeled Saccharomyces cerevisiae, Journal of Agricultural and Food Chemistry, vol.56, issue.24, pp.11792-11799, 2008.
DOI : 10.1021/jf8018479

E. R. Stadtman and R. L. Levine, Free radical-mediated oxidation of free amino acids and amino acid residues in proteins, Amino Acids, vol.25, issue.3-4, pp.207-218, 2003.
DOI : 10.1007/s00726-003-0011-2

A. J. Weids and C. M. Grant, The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress, Journal of Cell Science, vol.127, issue.6, pp.1327-1335, 2014.
DOI : 10.1242/jcs.144022
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3953820

R. A. Dunlop, P. A. Cox, S. A. Banack, and K. J. Rodgers, The Non-Protein Amino Acid BMAA Is Misincorporated into Human Proteins in Place of l-Serine Causing Protein Misfolding and Aggregation, PLoS ONE, vol.14, issue.9, p.75376, 2013.
DOI : 10.1371/journal.pone.0075376.g006

G. C. Scheper, M. S. Van-der-knaap, and C. G. Proud, Translation matters: protein synthesis defects in inherited disease, Nature Reviews Genetics, vol.114, issue.9, pp.711-723, 2007.
DOI : 10.1038/nrg2142

J. W. Lee, Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration, Nature, vol.613, issue.7107, pp.50-55, 2006.
DOI : 10.1016/S1097-2765(04)00126-1
URL : http://www.nature.com/nature/journal/v443/n7107/pdf/nature05096.pdf

D. Van-hoewyk, A tale of two toxicities: malformed selenoproteins and oxidative stress both contribute to selenium stress in plants, Annals of Botany, vol.112, issue.6, pp.965-972, 2013.
DOI : 10.1093/aob/mct163

B. Neuhierl and A. Bock, On the Mechanism of Selenium Tolerance in Selenium-Accumulating Plants. Purification and Characterization of a Specific Selenocysteine Methyltransferase from Cultured Cells of Astragalus Bisculatus, European Journal of Biochemistry, vol.1, issue.1, pp.235-238, 1996.
DOI : 10.1146/annurev.pp.20.060169.002355

D. R. Ellis, Production of Se-methylselenocysteine in transgenic plants expressing selenocysteine methyltransferase, BMC Plant Biology, vol.4, issue.1, p.1, 2004.
DOI : 10.1186/1471-2229-4-1

D. L. Leduc, Overexpression of Selenocysteine Methyltransferase in Arabidopsis and Indian Mustard Increases Selenium Tolerance and Accumulation, PLANT PHYSIOLOGY, vol.135, issue.1, pp.377-383, 2004.
DOI : 10.1104/pp.103.026989

A. Dimkovikj, B. Fisher, K. Hutchison, and D. Van-hoewyk, Stuck between a ROS and a hard place: Analysis of the ubiquitin proteasome pathway in selenocysteine treated Brassica napus reveals different toxicities during selenium assimilation, Journal of Plant Physiology, vol.181, pp.50-54, 2015.
DOI : 10.1016/j.jplph.2015.04.003

M. Wallenberg, Selenium induces a multi-targeted cell death process in addition to ROS formation, Journal of Cellular and Molecular Medicine, vol.20, issue.4, pp.671-684, 2014.
DOI : 10.1111/jcmm.12214

D. L. Hatfield and V. N. Gladyshev, The Outcome of Selenium and Vitamin E Cancer Prevention Trial (SELECT) Reveals the Need for Better Understanding of Selenium Biology, Molecular Interventions, vol.9, issue.1, pp.18-21, 2009.
DOI : 10.1124/mi.9.1.6

L. Decourty, Long Open Reading Frame Transcripts Escape Nonsense-Mediated mRNA Decay in Yeast, Cell Reports, vol.6, issue.4, pp.593-598, 2014.
DOI : 10.1016/j.celrep.2014.01.025
URL : https://hal.archives-ouvertes.fr/pasteur-01404015

C. Malabat and C. Saveanu, Identification of Links Between Cellular Pathways by Genetic Interaction Mapping (GIM), Methods Mol. Biol, vol.1361, pp.325-343, 2016.
DOI : 10.1007/978-1-4939-3079-1_18
URL : https://hal.archives-ouvertes.fr/pasteur-01427613