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1 UNIVERSITÉ DE STRASBOURG ÉCOLE DOCTORALE des Sciences de la Vie et de la Sante IGBMC - CNRS UMR Inserm U 964 THÈSE présentée par : Amita SINGH soutenue le : 29 Septembre 2014 pour obtenir le grade de : té de Strasbourg Discipline/ Spécialité : Sciences du Vivant/Aspects Moléculaires et Cellulaires de la Biologie THÈSE dirigée par : EGLY Jean-Marc DRE INSERM, IGBMC, Strasbourg (Fr) RAPPORTEURS : SCHAEFFER Laurent GELI Vincent LAUGEL Vincent DR, LBMC, Lyon (Fr) DR, CRCM, Marseille (Fr) PUPH, CHU de Strasbourg (Fr) 1
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123 Figure 2 Fold induction XPB wt XPB/ F99S XPB/ T119P p8/ttd-a wt p8/ttd-a (XP/CS) (TTD) (TTD) 20 A1 20 B1 20 C1 20 D1 20 E wt mut 0.4 A2 0.4 B2 0.4 C2 1 D2 0.5 E2 Fold induction % Input % Input % Input A3 0.4 B3 0.4 C3 1 D A4 0.4 B4 0.4 C4 1 D4 0.5 E Time(h) Time(h) Time(h) Time(h) XPD wt XPD/ R112H XPD/ G602D XPD/ R683W XPD/ R722W (TTD) (XP/CS) (XP) (TTD) 6 F1 90 G1 30 H1 80 I1 40 J E Time(h) RAR polii TFIIB XPD XPB p44 Cdk7 XPA XPG XPF CTCF wt Trans Non-trans 4 F2 4 G2 2 H2 10 I2 5 J2 % Input RAR polii TFIIB % Input 4 F3 4 G3 2 H3 10 I3 5 J XPD XPB p44 Cdk7 % Input F G4 2 H4 5 I4 5 J XPA XPG XPF CTCF Time(h) Time(h) Time(h) Time(h) Time(h) 123
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125 Figure 3 Fold induction % Input % Input Fold induction % Input % Input 10 5 A1 A2 A3 F1 F2 F3 XPB wt XPD wt 10 5 XPB/ F99S XPB/ T119P p8/ttd-a wt (XP/CS) (TTD) B1 10 C1 10 D1 10 E B2 1 C2 D2 E2 0 6 B3 20 C3 D3 E3 XPD/ R112H (TTD) XPD/ G602D (XP/CS) XPD/ R683W (XP) G1 H1 15 I1 15 J1 G2 H2 I2 J2 G3 20 H3 20 I3 20 J Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) p8/ttd-a (TTD) Time(h) XPD/ R722W (TTD) Time(h) Histone PTMs H3K9ac H3K9me2 H3K4me2 DNA breaks DNA demethyl Histone PTMs H3K9ac H3K9me2 H3K4me2 DNA breaks DNA demethyl 125
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127 Figure 4 Pro TATA M1 Ter RAR -65kb kb +323kb RARβ2 Interaction frequency XPB wt XPB/ F99S XPB/ T119P p8/ttd-a wt p8/ttd-a (XP/CS) (TTD) (TTD) 0.3 A 0.3 B 0.3 C 0.3 D 0.3 E Time(h) Time(h) Time(h) Time(h) Time(h) -65/Ter PRO/Ter M1/Ter +323/Ter Interaction frequency 0.3 F XPD wt 0.3 G XPD/ R112H (TTD) 0.9 H XPD/ G602D (XP/CS) 0.3 I XPD/ R683W (XP) Time(h) Time(h) Time(h) Time(h) XPD/ R722W (TTD) 0.3 J Time(h) -65/Ter PRO/Ter M1/Ter +323/Ter 127
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129 Figure 5 A Phosphorylation Transcription B Transcription C IIH6 XPBwt IIH6 XPB/F99S IIH6 XPB/T119P XPD CAK TFIIH IIH6 XPBwt XPDwt XPD/R112H XPD/G602D XPD/R683W XPD/R722W CAK XPDwt XPD/R112H XPD/G602D XPD/R683W XPD/R722W IIO IIA 309nt 309nt D XPB wt XPB/ F99S XPB/ T119P p8/ttd-a (XP/CS) (TTD) (TTD) 0.2 D1 0.2 D2 0.2 D3 0.2 D4 % Input Time(h) Time(h) Time(h) Time(h) XPD wt XPD/ R112H (TTD) XPD/ G602D (XP/CS) XPD/ R683W (XP) 1.4 D5 2.4 D6 1.4 D7 1.4 D8 1.4 D9 XPD/ R722W (TTD) % Input Time(h) Time(h) Time(h) Time(h) Time(h) 129
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131 Figure S1 XPB wt XPB/ F99S (XP/CS) XPB/ T119P (TTD) p8/ttd-a wt 0.4 A1 0.4 B1 0.4 C1 2 D1 2 E1 p8/ttd-a (TTD) % Input % Input % Input % Input % Input % Input A2 0.4 B2 0.4 C2 2 D2 2 E A3 0.4 B3 0.4 C3 D XPD wt XPD/ R112H XPD/ G602D XPD/ R683W XPD/ R722W (TTD) (XP/CS) (XP) (TTD) 4 F1 4 G1 2 H1 8 I1 10 J F2 4 G2 2 H2 8 I2 10 J F3 4 G3 2 H3 8 I3 10 J Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) Time(h) E Time(h) Time(h) RAR polii TFIIB XPD XPB p44 Cdk7 XPA XPG XPF CTCF RAR polii TFIIB XPD XPB p44 Cdk7 XPA XPG XPF CTCF 131
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133 Figure S2 DNA break at terminator region 1 XPB wt XPB/ F99S (XP/CS) XPB/ T119P (TTD) p8/ttd-a wt A 1 B 1 C 1 D 1 E p8/ttd-a (TTD) % Input % Input Time(h) Time(h) Time(h) Time(h) Time(h) XPD wt XPD/ R112H XPD/ G602D XPD/ R683W XPD/ R722W (TTD) (XP/CS) (XP) (TTD) 1 F 1 G 1 H 1 I 1 J Time(h) Time(h) Time(h) Time(h) Time(h) 133
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135 Figure S3 Pro TATA M1 Ter RAR -65kb kb +323kb RARβ2 Interaction frequency XPB wt 0 8 Time(h) XPB/ F99S (XP/CS) 0 6 Time(h) XPB/ T119P (TTD) 0 6 Time(h) p8/ttd-a wt 0.9 A 0.9 B 0.9 C 0.9 D 0.9 E Time(h) p8/ttd-a (TTD) 0 8 Time(h) -65/M1 PRO/M1 Ter/M1 +323/M1 Interaction frequency F XPD wt 0 8 Time(h) XPD/ R112H (TTD) XPD/ G602D (XP/CS) XPD/ R683W (XP) XPD/ R722W (TTD) 0.9 G 0.9 H 0.9 I 0.9 J Time(h) Time(h) Time(h) Time(h) -65/M1 PRO/M1 Ter/M1 +323/M1 135
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176 Résumé en Français de protéines autour du promoteur. Parmi ces protéines, le complexe TFIIH joue un rôle central et important au travers de ses sous-unités enzymatiques. Des mutations dans les sous-unités XPB, XPD et p8/ttd-a de TFIIH conduisent à trois maladies autosomiques récessives distinctes : xeroderma pigmentosum (XP), parfois associés avec le syndrome de Cockayne (XP/CS) et la trichothiodystrophie (TTD). En étudiant différentes mutations dans ces trois sousunités de TFIIH, nous avons montré que chaque mutation analysée conduit à une dérégulation transcriptionnelle spécifique du gène RAR2, gène cible des RAR. enzymatique de TFIIH conditionne le bon recrutement du complexe TFIIH et également des facteurs de réparation par excision de nucléotides (NER). TFIIH muté perturbe leur recrutement et par conséquence compromet le remodelage de la chromatine médiée par les facteurs NER tels que les modifications post- s boucles de chromatine. Par conséquence, en plus de ses activités enzymatiques, TFIIH forme une plate-forme afin de recruter les facteurs NER et orchestres les fonctions connexes de la transcription. Cette pénétrance variable parmi les mutants donne lieu à un gradient de phénotype observé chez les patients TTD, XP ou XP/CS. Mot-clés : TFIIH, NER, transcription, chromatine Résumé en anglais Amita SINGH Contribution de TFIIH dans le remodelage de la chromatine dépendant des facteurs NER lors de la transcription Fidelity in transcription of the gene requires assembly of set of proteins around the promoter, upon gene activation. The TFIIH complex is central among these proteins and plays a key role through its enzymatic subunits. Mutations in TFIIH subunits XPB, XPD and p8/ttd-a leads to three distinct autosomal recessive disorders: xeroderma pigmentosum (XP), sometimes different mutation in these three subunits of TFIIH from mentioned genetic disease models, we have shown that each mutation analyzed led to a specific transcriptional dysregulation of the RAR-target gene RAR 2. The architectural and enzymatic integrity of TFIIH condition the appropriate recruitment of TFIIH complex and further the arrival of the Nucleotide Excision Repair (NER) factors. By disturbing their recruitment, mutated TFIIH consequently compromised the chromatin remodeling mediated by NER factors such as histones posttranslational modifications (PTMs), DNA breaks induction, DNA demethylation and gene looping. Hence it can be concluded that in addition to its enzymatic activities, TFIIH provide a platform to recruit the NER factors and orchestrates the related functions in transcription. Such varying penetrance among mutants gives rise to a phenotype gradient as observed in TTD, XP or XP/CS patients. Keywords: TFIIH, NER, transcription, chromatin. 176
Transcrip)on Regula)on And Gene Expression in Eukaryotes Cycle G2 (lecture 13709) FS 2014 P Ma?hias & RG Clerc
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