## 3 Experimental Section
### ChIP Experiments  
The fifth instar day-3 larvae fat bodies were treated with 1\(\times\) cold phosphate-buffered saline (PBS) containing 1% protease inhibitor cocktail (Roche, Basel, Switzerland). To cross-link samples, a formaldehyde solution (50 mM HEPES-KOH [pH 7.5], 100 mM NaCl, 1 mM EDTA [pH 8.0], 0.5 mM EGTA [pH 8.0], 11% formaldehyde) was added to a final concentration of 1% for 15 min at room temperature. Eggs were masked with a pestle in the formaldehyde solution to prepare samples for ChIP experiments. The reaction was stopped by adding a glycine solution to a final concentration of 125 mM for 5 min at room temperature and washed twice with 1\(\times\) cold PBS. The fixed fat bodies were disrupted with a Polytron (KINEMATICA, Lucern, Switzerland) (10,000 rpm, 20 s) and centrifuged at 2800 rpm for 5 min at 4 \({}^{\circ}\)C. The samples were resuspended in lysis buffer (10 mM Tris-HCl [pH 8.0], \begin{table}
\begin{tabular}{c c c} \hline
**Target gene** & **Primers** & **Sequence (5’ to 3’)** \\ \hline _EF-1_ I12 & EF-1112F1 & GCATTAATATTAATTCCACCACAAG \\ _Bm-Sxl_ & EF-1112R1 & CACACCTCACTGCTCTCTCCGC \\ _Bm-Sxl_ & Sxli1F1 & GGCTAAACTATCTTCAACAAG \\ promoter & Sxli1R1 & CGGTCCACCGTTCTGTGGAAAAG \\ _Bm-Sxl_ E1 & Sxle1F1 & GCAGTGCCAATGGACGAATC \\  & Sxle1R1 & GTTCACTGACTTTGGAGTAG \\ _Bm-Sxl_ E2 & Sxle2F1 & GCCTACTCGAACAAATAAAAAG \\  & Sxle2R1 & TTCCAAAGAATTGAACTCTG \\ _Bm-Sxl_ I2 & Sxli2F1 & TGAATCAGAAACATCTCTATTGG \\  & Sxli2R1 & CCAAGCCGCTGCCTACCTAAC \\ _Bm-Sxl_ E3 & Sxle3F1 & CGAGGAGGGGGTTCGAAAC \\  & Sxle3R1 & CCTTCACTACTCGACAGCTCTC \\ _BmIMP_ & IMPE2F1 & ATCCCAAAGGTACTCATCAG \\ Proximal & IMPE212R & GCATGCATACCTCAACAATAC \\ _BmIMP_ Distal & IMPE7F2 & GGATCATGGGGCAAAGGGGGAC \\  & IMPI7R2 & AGACACTTGATTCCATACC \\ _EF-1_ Proximal & EF-1E2F1 & TGGCGATGGAGGCGGAGAAGG \\  & EF-112R1 & GAAAAAGAAGAAGCATTCATGC \\ _EF-1_ Distal & EF-111E12F & ATGATACTGTATTAACTGCATTC \\  & EF-1E12R2 & TTCAGGATTTTGAGACCCTG \\  & IMPE7F1 & ATGCGGGAAGAGGTTTTATG \\ _BmIMP_ E7-E8 & BmIMPR1 & TCATCCCGCCTCAGACGATTG \\  & BmIMPF1 & ATGGACGGTGCATGTCTCAAG \\ _BmIMP_ E1-E3 & IMPE3R1 & CATCCATTCAACCCGTTTTATG \\  & BmIMPF1 & ATGGACGGTACATGTCTCAAG \\ _BmIMP_ E1S & IMPE2R2 & GCCTGCTCTGGACTCTCGAAAG \\  & IMPE1 LF1 & AATCTGCTAAAATGGGGAAG \\  & IMPE2R2 & GCCTGCTCTGGACTCTCGAAAG \\  & BmSxlF2 & ACTGCGGTTCCTATTTAAC \\ _Bm-Sxl_ S & BmSxlSR1 & GTACTGCGTTTGATTGGTC \\  & BmSxlF2 & ACTGCGGTACCTATTTAAC \\  & BmSxlLR1 & CTGCGTTTGATTTGATTTTC \\ \hline \end{tabular}
\end{table} 
Table 4: _Cont._100 mM NaCl, 1 mM EDTA [pH 8.0], 0.5 mM EGTA [pH 8.0], 0.1% Na-deoxycholate, 0.5% _N_-lauroylsarcosine, 1% protease inhibitor) and sonicated (pulsed 30 s, paused 1 min \(\times\) 7 sets) on ice to avoid overheating. Triton-X was added to the resulting lysate at a final concentration of 1% and centrifuged at 15,000 rpm for 10 min at 4 \({}^{\circ}\)C. An aliquot (200 \(\upmu\)L) of each sonicated sample served as an input DNA control. For ChIP, 300 \(\upmu\)L of the supernatant was incubated with Dynabeads Protein G (Invitrogen, Carlsbad, CA, USA) with the appropriate antibody overnight at 4 \({}^{\circ}\)C. The beads were washed twice with 1\({}^{\times}\) cold PBS. Next, 5 \(\upmu\)g of antibodies were added in 300-\(\upmu\)L blocking solution (0.5% bovine serum albumin [BSA]/PBS) and incubated overnight at 4 \({}^{\circ}\)C. The antibodies used in this study were anti-H3 antibody (ab1791, Abcam, Cambridge, UK), anti-H3K36 me3 antibody (ab9050, Abcam, Cambridge, UK), anti-H3K79 me2 antibody (ab3594, Abcam, Cambridge, UK), and anti-rabbit IgG antibody (12-370, Millipore, Billerica, MA, USA). The beads were washed once with low salt buffer (20 mM Tris-HCl [pH 8.0], 150 mM NaCl, 2 mM EDTA [pH 8.0], 0.1% SDS, 1% Triton X-100), twice with high salt buffer (20 mM Tris-HCl [pH 8.0], 400 mM NaCl, 2 mM EDTA [pH 8.0], 0.1% SDS, 1% Triton X-100), five times with RIPA buffer (50 mM HEPES-KOH [pH 7.5], 500 mM LiCl, 1 mM EDTA [pH 8.0], 1% NP-40, 0.7% Na-deoxycholate), and once with TE (Tris + EDTA) + 50 mM NaCl.