M. Muller-mcnicoll and K. M. Neugebauer, How cells get the message: dynamic assembly and function of mRNA???protein complexes, Nature Reviews Genetics, vol.24, issue.4, pp.275-287, 2013.
DOI : 10.1016/S1097-2765(03)00089-3

R. Luna, A. G. Rondon, and A. Aguilera, New clues to understand the role of THO and other functionally related factors in mRNP biogenesis, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, vol.1819, issue.6, pp.514-520, 2012.
DOI : 10.1016/j.bbagrm.2011.11.012

M. Oeffinger and D. Zenklusen, To the pore and through the pore: A story of mRNA export kinetics, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, vol.1819, issue.6, pp.494-506, 2012.
DOI : 10.1016/j.bbagrm.2012.02.011

S. Chavez, T. Beilharz, A. G. Rondon, H. Erdjument-bromage, P. Tempst et al., A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae, The EMBO Journal, vol.19, issue.21, pp.5824-5834, 2000.
DOI : 10.1093/emboj/19.21.5824

A. Pena, K. Gewartowski, S. Mroczek, J. Cuellar, A. Szykowska et al., Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor, The EMBO Journal, vol.22, issue.6, pp.1605-1616, 2012.
DOI : 10.1038/emboj.2012.10

D. Zenklusen, P. Vinciguerra, J. C. Wyss, and F. Stutz, Stable mRNP Formation and Export Require Cotranscriptional Recruitment of the mRNA Export Factors Yra1p and Sub2p by Hpr1p, Molecular and Cellular Biology, vol.22, issue.23, pp.8241-8253, 2002.
DOI : 10.1128/MCB.22.23.8241-8253.2002

K. Strasser, S. Masuda, P. Mason, J. Pfannstiel, M. Oppizzi et al., TREX is a conserved complex coupling transcription with messenger RNA export, Nature, vol.8, issue.6886, pp.304-308, 2002.
DOI : 10.1038/21239

E. Hurt, M. J. Luo, S. Rother, R. Reed, and K. Strasser, Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex, Proc. Natl Acad. Sci. USA, pp.1858-1862, 2004.
DOI : 10.1073/pnas.0308663100

S. Hacker and H. Krebber, Differential Export Requirements for Shuttling Serine/Arginine-type mRNA-binding Proteins, Journal of Biological Chemistry, vol.279, issue.7, pp.5049-5052, 2004.
DOI : 10.1074/jbc.C300522200

C. Gwizdek, N. Iglesias, M. S. Rodriguez, B. Ossareh-nazari, M. Hobeika et al., Ubiquitin-associated domain of Mex67 synchronizes recruitment of the mRNA export machinery with transcription, Proc. Natl Acad. Sci. USA, pp.16376-16381, 2006.
DOI : 10.1073/pnas.0607941103

URL : https://hal.archives-ouvertes.fr/hal-00111711

S. Guo, M. A. Hakimi, D. Baillat, X. Chen, M. J. Farber et al., Linking transcriptional elongation and messenger RNA export to metastatic breast cancers, Cancer Res, vol.65, pp.3011-3016, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00171955

M. S. Dominguez-sanchez, S. Barroso, B. Gomez-gonzalez, R. Luna, and A. Aguilera, Genome Instability and Transcription Elongation Impairment in Human Cells Depleted of THO/TREX, PLoS Genetics, vol.16, issue.12, p.1002386, 2011.
DOI : 10.1371/journal.pgen.1002386.s009

D. Libri, K. Dower, J. Boulay, R. Thomsen, M. Rosbash et al., Interactions between mRNA Export Commitment, 3'-End Quality Control, and Nuclear Degradation, Molecular and Cellular Biology, vol.22, issue.23, pp.8254-8266, 2002.
DOI : 10.1128/MCB.22.23.8254-8266.2002

M. Rougemaille, R. K. Gudipati, J. R. Olesen, R. Thomsen, B. Seraphin et al., Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants, The EMBO Journal, vol.22, issue.9, pp.2317-2326, 2007.
DOI : 10.1038/sj.emboj.7601669

URL : https://hal.archives-ouvertes.fr/hal-00167518

Y. Li, X. Wang, X. Zhang, and D. W. Goodrich, Human hHpr1/p84/Thoc1 Regulates Transcriptional Elongation and Physically Links RNA Polymerase II and RNA Processing Factors, Molecular and Cellular Biology, vol.25, issue.10, pp.4023-4033, 2005.
DOI : 10.1128/MCB.25.10.4023-4033.2005

V. Voynov, K. J. Verstrepen, A. Jansen, V. M. Runner, S. Buratowski et al., Genes with internal repeats require the THO complex for transcription, Proc. Natl Acad. Sci. USA, pp.14423-14428, 2006.
DOI : 10.1073/pnas.0606546103

B. Gomez-gonzalez, M. Garcia-rubio, R. Bermejo, H. Gaillard, K. Shirahige et al., Genome-wide function of THO/TREX in active genes prevents R-loop-dependent replication obstacles, The EMBO Journal, vol.1799, issue.15, pp.3106-3119, 2011.
DOI : 10.1128/MCB.22.23.8241-8253.2002

S. Jimeno, A. G. Rondon, R. Luna, and A. Aguilera, The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability, The EMBO Journal, vol.21, issue.13, pp.3526-3535, 2002.
DOI : 10.1093/emboj/cdf335

P. Huertas and A. Aguilera, Cotranscriptionally Formed DNA:RNA Hybrids Mediate Transcription Elongation Impairment and Transcription-Associated Recombination, Molecular Cell, vol.12, issue.3, pp.711-721, 2003.
DOI : 10.1016/j.molcel.2003.08.010

P. C. Stirling, Y. A. Chan, S. W. Minaker, M. J. Aristizabal, I. Barrett et al., R-loop-mediated genome instability in mRNA cleavage and polyadenylation mutants, Genes & Development, vol.26, issue.2, pp.163-175, 2012.
DOI : 10.1101/gad.179721.111

M. B. Fasken and A. H. Corbett, Mechanisms of nuclear mRNA quality control, RNA Biology, vol.6, issue.3, pp.237-241, 2009.
DOI : 10.4161/rna.6.3.8330

M. Schmid and T. H. Jensen, Transcription-associated quality control of mRNP, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, vol.1829, issue.1, pp.158-168, 2013.
DOI : 10.1016/j.bbagrm.2012.08.012

K. Strasser and E. Hurt, Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p, Nature, vol.84, issue.6856, pp.648-652, 2001.
DOI : 10.1038/35098113

G. M. Hautbergue, M. L. Hung, A. P. Golovanov, L. Y. Lian, and S. A. Wilson, Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP, Proc. Natl Acad. Sci. USA, pp.5154-5159, 2008.
DOI : 10.1073/pnas.0709167105

E. Tutucci and F. Stutz, Keeping mRNPs in check during assembly and nuclear export, Nature Reviews Molecular Cell Biology, vol.277, issue.6, pp.377-384, 2011.
DOI : 10.1038/nrm3119

N. Iglesias, E. Tutucci, C. Gwizdek, P. Vinciguerra, V. Dach et al., Ubiquitin-mediated mRNP dynamics and surveillance prior to budding yeast mRNA export, Genes & Development, vol.24, issue.17, pp.1927-1938, 2010.
DOI : 10.1101/gad.583310

URL : https://hal.archives-ouvertes.fr/hal-00518145

R. Geiss-friedlander and F. Melchior, Concepts in sumoylation: a decade on, Nature Reviews Molecular Cell Biology, vol.1773, issue.12, pp.947-956, 2007.
DOI : 10.1038/nrm2293

V. Vethantham and J. L. Manley, Emerging Roles for SUMO in mRNA Processing and Metabolism, SUMO Regulation of Cellular Processes, pp.41-57, 2009.
DOI : 10.1007/978-90-481-2649-1_3

J. O. Rouviere, M. C. Geoffroy, and B. Palancade, Multiple crosstalks between mRNA biogenesis and SUMO, Chromosoma, vol.279, issue.31, pp.387-399, 2013.
DOI : 10.1007/s00412-013-0408-y

J. R. Gareau and C. D. Lima, The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition, Nature Reviews Molecular Cell Biology, vol.8, issue.12, pp.861-871, 2010.
DOI : 10.1038/nrm3011

D. M. Green, C. P. Johnson, H. Hagan, and A. H. Corbett, The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export, Proc. Natl Acad. Sci. USA, pp.1010-1015, 2003.
DOI : 10.1073/pnas.0336594100

P. Vinciguerra, N. Iglesias, J. Camblong, D. Zenklusen, and F. Stutz, Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export, The EMBO Journal, vol.110, issue.4, pp.813-823, 2005.
DOI : 10.1128/MCB.22.23.8241-8253.2002

X. Zhao, C. Y. Wu, and G. Blobel, Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality, The Journal of Cell Biology, vol.7, issue.4, pp.605-611, 2004.
DOI : 10.1128/MCB.22.18.6498-6508.2002

B. Palancade and V. Doye, Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties?, Trends in Cell Biology, vol.18, issue.4, pp.174-183, 2008.
DOI : 10.1016/j.tcb.2008.02.001

A. R. Fernandes, N. P. Mira, R. C. Vargas, I. Canelhas, and I. Sa-correia, Saccharomyces cerevisiae adaptation to weak acids involves the transcription factor Haa1p and Haa1p-regulated genes, Biochemical and Biophysical Research Communications, vol.337, issue.1, pp.95-103, 2005.
DOI : 10.1016/j.bbrc.2005.09.010

M. Oeffinger, K. E. Wei, R. Rogers, J. A. Degrasse, B. T. Chait et al., Comprehensive analysis of diverse ribonucleoprotein complexes, Nature Methods, vol.148, issue.11, pp.951-956, 2007.
DOI : 10.1038/nmeth1101

M. Rougemaille, G. Dieppois, E. Kisseleva-romanova, R. K. Gudipati, S. Lemoine et al., THO/Sub2p Functions to Coordinate 3???-End Processing with Gene-Nuclear Pore Association, Cell, vol.135, issue.2, pp.308-321, 2008.
DOI : 10.1016/j.cell.2008.08.005

C. Gwizdek, M. Hobeika, B. Kus, B. Ossareh-nazari, C. Dargemont et al., The mRNA Nuclear Export Factor Hpr1 Is Regulated by Rsp5-mediated Ubiquitylation, Journal of Biological Chemistry, vol.280, issue.14, pp.13401-13405, 2005.
DOI : 10.1074/jbc.C500040200

K. C. Abruzzi, S. Lacadie, and M. Rosbash, Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes, The EMBO Journal, vol.264, issue.13, pp.2620-2631, 2004.
DOI : 10.1038/35030160

J. Mouaikel, S. Z. Causse, M. Rougemaille, Y. Daubenton-carafa, C. Blugeon et al., High-Frequency Promoter Firing Links THO Complex Function to Heavy Chromatin Formation, Cell Reports, vol.5, issue.4, pp.1082-1094, 2013.
DOI : 10.1016/j.celrep.2013.10.013

H. D. Ulrich and A. A. Davies, In Vivo Detection and Characterization of Sumoylation Targets in Saccharomyces cerevisiae, Methods Mol. Biol, vol.497, pp.81-103, 2009.
DOI : 10.1007/978-1-59745-566-4_6

L. Jourdren, A. Duclos, C. Brion, T. Portnoy, H. Mathis et al., Teolenn: an efficient and customizable workflow to design high-quality probes for microarray experiments, Nucleic Acids Research, vol.38, issue.10, p.117, 2010.
DOI : 10.1093/nar/gkq110

S. Lemoine, F. Combes, N. Servant, L. Crom, and S. , Goulphar: rapid access and expertise for standard two-color microarray normalization methods, BMC Bioinformatics, vol.7, issue.1, p.467, 2006.
DOI : 10.1186/1471-2105-7-467

URL : https://hal.archives-ouvertes.fr/inserm-00122139

A. Chadrin, B. Hess, M. San-roman, X. Gatti, B. Lombard et al., Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution, The Journal of Cell Biology, vol.10, issue.5, pp.795-811, 2010.
DOI : 10.1083/jcb.200910043.dv

URL : https://hal.archives-ouvertes.fr/hal-00504296

J. I. Piruat and A. Aguilera, Mutations in the yeast SRB2 general transcription factor suppress hpr1-induced recombination and show defects in DNA repair, Genetics, vol.143, pp.1533-1542, 1996.

A. Lewis, R. Felberbaum, and M. Hochstrasser, A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance, The Journal of Cell Biology, vol.35, issue.5, pp.813-827, 2007.
DOI : 10.1083/jcb.200405168

M. Niepel, C. Strambio-de-castillia, J. Fasolo, B. T. Chait, and M. P. Rout, The nuclear pore complex???associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly, The Journal of Cell Biology, vol.109, issue.2, pp.225-235, 2005.
DOI : 10.1091/mbc.E02-10-0655

M. Niepel, K. R. Molloy, R. Williams, J. C. Farr, A. C. Meinema et al., The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome, Molecular Biology of the Cell, vol.24, issue.24, pp.3920-3938, 2013.
DOI : 10.1091/mbc.E13-07-0412

E. Garcia-oliver, V. Garcia-molinero, and S. Rodriguez-navarro, mRNA export and gene expression: The SAGA???TREX-2 connection, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, vol.1819, issue.6, pp.555-565
DOI : 10.1016/j.bbagrm.2011.11.011

K. Bielska, J. Seliga, E. Wieczorek, S. Kedracka-krok, R. Niedenthal et al., Alternative sumoylation sites in the Drosophila nuclear receptor Usp, The Journal of Steroid Biochemistry and Molecular Biology, vol.132, issue.3-5, pp.227-238, 2012.
DOI : 10.1016/j.jsbmb.2012.05.011

C. Maison, D. Bailly, D. Roche, R. Montes-de-oca, A. V. Probst et al., SUMOylation promotes de novo targeting of HP1?? to pericentric heterochromatin, Nature Genetics, vol.7, issue.3, pp.220-227, 2011.
DOI : 10.1002/pmic.200600784

URL : https://hal.archives-ouvertes.fr/hal-00685744

C. Figueroa-romero, J. A. Iniguez-lluhi, J. Stadler, C. R. Chang, D. Arnoult et al., SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle, The FASEB Journal, vol.23, issue.11, pp.3917-3927, 2009.
DOI : 10.1096/fj.09-136630

P. Radivojac, V. Vacic, C. Haynes, R. R. Cocklin, A. Mohan et al., Identification, analysis, and prediction of protein ubiquitination sites, Proteins: Structure, Function, and Bioinformatics, vol.50, issue.2, pp.365-380, 2010.
DOI : 10.1002/prot.22555

H. Xie, S. Vucetic, L. M. Iakoucheva, C. J. Oldfield, A. K. Dunker et al., Functional Anthology of Intrinsic Disorder. 3. Ligands, Post-Translational Modifications, and Diseases Associated with Intrinsically Disordered Proteins, Journal of Proteome Research, vol.6, issue.5, pp.1917-1932, 2007.
DOI : 10.1021/pr060394e

B. Gomez-gonzalez, I. Felipe-abrio, and A. Aguilera, The S-Phase Checkpoint Is Required To Respond to R-Loops Accumulated in THO Mutants, Molecular and Cellular Biology, vol.29, issue.19, pp.5203-5213, 2009.
DOI : 10.1128/MCB.00402-09

N. P. Mira, J. D. Becker, and I. Sa-correia, Response to Acetic Acid, OMICS: A Journal of Integrative Biology, vol.14, issue.5, pp.587-601, 2010.
DOI : 10.1089/omi.2010.0048

N. P. Mira, M. C. Teixeira, and I. Sa-correia, : A Genome-Wide View, OMICS: A Journal of Integrative Biology, vol.14, issue.5, pp.525-540, 2010.
DOI : 10.1089/omi.2010.0072

U. Hardeland, R. Steinacher, J. Jiricny, and P. Schar, Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover, The EMBO Journal, vol.248, issue.6, pp.1456-1464, 2002.
DOI : 10.1093/emboj/21.6.1456

M. T. Vassileva and M. J. Matunis, SUMO Modification of Heterogeneous Nuclear Ribonucleoproteins, Molecular and Cellular Biology, vol.24, issue.9, pp.3623-3632, 2004.
DOI : 10.1128/MCB.24.9.3623-3632.2004

J. L. Parker, A. Bucceri, A. A. Davies, K. Heidrich, H. Windecker et al., SUMO modification of PCNA is controlled by DNA, The EMBO Journal, vol.376, issue.18, pp.2422-2431, 2008.
DOI : 10.1038/emboj.2008.162

I. Psakhye and S. Jentsch, Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair, Cell, vol.151, issue.4, pp.807-820, 2012.
DOI : 10.1016/j.cell.2012.10.021

R. T. Hay, SUMO, Molecular Cell, vol.18, issue.1, pp.1-12, 2005.
DOI : 10.1016/j.molcel.2005.03.012

URL : https://hal.archives-ouvertes.fr/hal-00479165

S. Ramachandran, D. D. Tran, S. Klebba-faerber, C. Kardinal, A. D. Whetton et al., An ataxia-telangiectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5, RNA, vol.17, issue.11, pp.1957-1966, 2011.
DOI : 10.1261/rna.2820911

T. Makhnevych, C. Ptak, C. P. Lusk, J. D. Aitchison, and R. W. Wozniak, The role of karyopherins in the regulated sumoylation of septins, The Journal of Cell Biology, vol.4, issue.1, pp.39-49, 2007.
DOI : 10.1074/jbc.M401541200

Y. Sydorskyy, T. Srikumar, S. M. Jeram, S. Wheaton, F. J. Vizeacoumar et al., A Novel Mechanism for SUMO System Control: Regulated Ulp1 Nucleolar Sequestration, Molecular and Cellular Biology, vol.30, issue.18, pp.4452-4462, 2010.
DOI : 10.1128/MCB.00335-10

S. A. Johnson, G. Cubberley, and D. L. Bentley, Cotranscriptional Recruitment of the mRNA Export Factor Yra1 by Direct Interaction with the 3??? End Processing Factor Pcf11, Molecular Cell, vol.33, issue.2, pp.215-226, 2009.
DOI : 10.1016/j.molcel.2008.12.007

A. L. Mackellar and A. L. Greenleaf, Cotranscriptional Association of mRNA Export Factor Yra1 with C-terminal Domain of RNA Polymerase II, Journal of Biological Chemistry, vol.286, issue.42, pp.36385-36395, 2011.
DOI : 10.1074/jbc.M111.268144

M. Mollapour, D. Fong, K. Balakrishnan, N. Harris, S. Thompson et al., Screening the yeast deletant mutant collection for hypersensitivity and hyper-resistance to sorbate, a weak organic acid food preservative, Yeast, vol.21, issue.11, pp.927-946, 2004.
DOI : 10.1002/yea.1141

M. Kawahata, K. Masaki, T. Fujii, and H. Iefuji, cultures induce expression of intracellular metal metabolism genes regulated by Aft1p, FEMS Yeast Research, vol.6, issue.6, pp.924-936, 2006.
DOI : 10.1111/j.1567-1364.2006.00089.x

N. P. Mira, M. Palma, J. F. Guerreiro, and I. Sa-correia, Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid, Microbial Cell Factories, vol.9, issue.1, p.79, 2010.
DOI : 10.1186/1475-2859-9-79

J. Assenholt, J. Mouaikel, K. R. Andersen, D. E. Brodersen, D. Libri et al., Exonucleolysis is required for nuclear mRNA quality control in yeast THO mutants, RNA, vol.14, issue.11, pp.2305-2313, 2008.
DOI : 10.1261/rna.1108008