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SRX8349982: GSM4556261: Larp7 rep1; Mus musculus; RIP-Seq
1 ILLUMINA (Illumina HiSeq 2500) run: 6.7M spots, 324.7M bases, 164.8Mb downloads

Submitted by: NCBI (GEO)
Study: Nascent RNA antagonises the interaction of a set of regulatory proteins with chromatin
show Abstracthide Abstract
A number of regulatory factors are recruited to chromatin by specialised RNAs. Whether RNA has a more general role in regulating the interaction of proteins with chromatin has not been determined. We used proteomics methods to measure the global impact of nascent RNA on chromatin in embryonic stem cells. Surprisingly, we found that nascent RNA primarily antagonised the interaction of chromatin modifiers and transcriptional regulators with chromatin. Transcriptional inhibition and RNA degradation induced recruitment of a set of transcriptional regulators, chromatin modifiers, nucleosome remodelers, and regulators of higher-order structure. RNA directly bound to factors including BAF, NuRD, EHMT1 and INO80 and inhibited their interaction with nucleosomes. The transcriptional elongation factor P-TEFb directly bound pre-mRNA and its recruitment to chromatin upon Pol II inhibition was regulated by the 7SK ribonucleoprotein complex. We postulate that by antagonising the interaction of regulatory proteins with chromatin, nascent RNA links transcriptional output with chromatin composition. Overall design: iCLIP for P-TEFb, LARP7 and input in mESC treated with either DMSO or pla-B. Also RNA-seq from chromatin or whole cell extract from mESC treated with triptolide or flavopiridol for 0, 1, 3 or 9 hours and also from permeabilised mock or RNaseA-treated mESC. Total RNA and polyA+ RNA was sequenced from the chromatin fraction to measure mature polyA+ and nascent RNA associated with chromatin and polyA+ RNA was sequenced from the whole cell extract samples to measure mature polyA+ RNA.
Sample: Larp7 rep1
SAMN14933924 • SRS6666599 • All experiments • All runs
Organism: Mus musculus
Library:
Instrument: Illumina HiSeq 2500
Strategy: RIP-Seq
Source: TRANSCRIPTOMIC
Selection: other
Layout: SINGLE
Construction protocol: Individual-nucleotide resolution UV crosslinking and immunoprecipitation protocols were based in protocols available at Huppertz et al. Cells were irradiated with 0.2 J/cm2 of UV light in a Strataliker 2400 (Stratagene) with bulbs emitting at 254nm, and 6-10x107 cells per IP were lysed in 1mL of Lysis buffer. Lysates were syringed with a 27G needle and sonicated for 3x 10s pulses with a Diagenode Picoruptor. Lysates were incubated in a Thermomixer at 37°C and 1100 rpm for three minutes after addition of 200U/mL of DNase Turbo and of 20 U/mL of RNase I. IPs were set up using 5ug of antibody as previously described in the iCLIP protocol. Beads were washed 3x with 900 μl high-salt buffer (50 mM Tris-HCl, pH 7.4; 1 M NaCl; 1 mM EDTA; 1% NP-40; 0.1% SDS; 0.5% sodium deoxycholate and 1M Urea), 2x with 900 μl wash buffer (20 mM Tris-HCl, pH 7.4; 10 mM MgCl2; 0.2% Tween-20) resuspended in 20 μl PNK mix (15 μl water; 4 μl 5x PNK pH 6.5 buffer [350mM Tris-HCl, pH 6.5; 50mM MgCl2 25mM dithiothreitol]; 0.5 μl PNK enzyme; 0.5 μl RNasin [Promega]) and incubated 30 min at 37°C 1100 rpm. Beads were washed 3x with 900 μl high-salt buffer, 2x with 900 μl wash buffer, resuspended in beads in 20 μl ligation mix (9 μl water; 4 μl 4x ligation buffer [200 mM Tris-HCl; 40m mM MgCl2; 40 mM dithiothreitol]; 1 μl RNA ligase [NEB]; 0.5 μl RNasin [Promega]; 1.5 μl pre-adenylated linker L3 [20 μM]; 4 μl PEG400 [81170, Sigma]), ligation was performed over night at 16°C and 1100 rpm. Beads were washed 3x with high-salt buffer, 2x wash buffer and 20% of the beads were incubated with 8 μl of hot PNK mix (0.4 μl PNK [NEB]; 0.8 μl 32P-γ-ATP; 0.8 μl 10x PNK buffer [NEB]; 6 μl water), radiolabelled and non-radiolabelled beads were pooled again and resuspended in 20 μl in NuPAGE loading buffer with reducing agent and run on a 4-12% NuPAGE Bis-Tris gel (Invitrogen) in MOPS buffer according to the manufacturer's instructions. Protein-RNA complexes were transferred to a nitrocellμlose membrane (Hybond, GE Healthcare) washed 2x with 1x PBS and exposed to a Fuji film. Using the auto-radiograph as a mask RNA-protein complexes attached to the membrane were isolated and treated with 200 μl PK buffer (100 mM Tris-HCl pH 7.4; 50 mM NaCl; 10 mM EDTA) and 10 μl proteinase K (Roche, 03115828001) for 20 minutes at 1,100 rpm and 37°C. 200 μl of PK urea buffer (100 mM Tris-HCl pH 7.4; 50 mM NaCl; 10 mM EDTA; 7 M urea) was added and a second incubation was performed for 20 minutes at 37°C and 1100 rpm. Solution was collected and RNA was isolated by phenol:chloroform extraction and ethanol precipitation overnight at -20°C. RNA pellet was resuspended in 7.25 μl RNA/primer mix (6.25 μl water; 0.5 μll Rclip primer [0.5 uM]; 0.5 μl dNTP mix [10mM]) and transferred in a 0.2 ml tube and incubated at 70°C. Reverse transcription was performed by addition of 2 μl 5x RT buffer; 0.5 μl 0.1M DTT; 0.25 μl Superscript III reverse transcriptase [Invitrogen] and incubation for 20 min at 42°C, 40 min at 50°C and 5 min at 80°C. cDNA was fractionated by running samples on a precast 6% TBE-urea gel at 180 V 40 min and isolating bands at 120-180 nt (high), 85-120 nt (medium) and 70-85 nt (low). Gel slices were submerged and crushed in TE buffer, incubated 1h at 37°C 1100 rpm, flash frozen, and a second incubation was performed 1h at 37°C 1100 rpm. cDNA was isolated by phenol:chloroform extraction and ethanol precipitation overnight at -20°C. cDNA was resuspended in 8 μl ligation mix (6.5 μl water; 0.8 μl 10x CircLigase Buffer II; 0.4 μl 50 mM MnCl2; 0.3 μl; Circligase II [Epicentre]) transferred into a 0.2ml tube and incubated for 1 h at 60°C for circularization. Samples were incubated in 30 μl oligo annealing mix (26 μl water; 3 μl FastDigest Buffer [Fermentas]; 1 μl cut_oligo [10 μM]), the oligo was annealed in a decreasing temperature gradient and circular cDNA re-linearized by incubating samples with 2 μl BamHI (Fast Fermentas). cDNA was isolated by phenol:chloroform extraction and ethanol precipitation overnight at -20°C and the pellet resuspended in 20 μl of H20. Amplification was performed using 10 μl cDNA; 1 μl primer mix P5/P3 solexa (10 μM each); 20 μl Accuprime Supermix 1 enzyme [Invitrogen], 9 μl H20 and the following PCR programme: 94°C for 2 min, [94°C for 15 sec, 65°C for 30 sec, 68°C for 30 sec]n cycles, 68°C for 3 min, 4°C, with a number of cycles optimized previously. Library integrity was analysed using 8 μl PCR product with 8 μl of 5x TBE loading buffer and loading on a precast 6% TBE gel (Invitrogen). Gel was stained with Sybrgreen I (Invitrogen) and analyse with a gel imager. Library concentration was determined using a KAPA kit according to the manufacturer's instructions.
Experiment attributes:
GEO Accession: GSM4556261
Links:
Runs: 1 run, 6.7M spots, 324.7M bases, 164.8Mb
Run# of Spots# of BasesSizePublished
SRR117985046,736,361324.7M164.8Mb2021-06-24

ID:
10860940

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