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PBRM1 bromodomains associate with RNA to facilitate chromatin association

ABSTRACT: PBRM1 bromodomains associate with RNA to facilitate chromatin association

PROVIDER: PRJNA915086 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22869203_1.fastq.gz	Fastqsanger.gz
	SRR22869203_2.fastq.gz	Fastqsanger.gz
	SRR22869204_1.fastq.gz	Fastqsanger.gz
	SRR22869204_2.fastq.gz	Fastqsanger.gz
	SRR22869205_1.fastq.gz	Fastqsanger.gz

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PBRM1 bromodomains associate with RNA to facilitate chromatin association (CLIP-seq)

Project description:PBRM1 bromodomains associate with RNA to facilitate chromatin association (CLIP-seq)

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PBRM1 bromodomains associate with RNA to facilitate chromatin association (ChIP-seq)

Project description:PBRM1 bromodomains associate with RNA to facilitate chromatin association (ChIP-seq)

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PBRM1 bromodomains associate with RNA to facilitate chromatin association (CLIP-seq)

Project description:PBRM1 is a subunit of the PBAF chromatin remodeling complex, which is mutated in 40-50% of clear cell renal cell carcinoma patients. It is thought to largely function as a chromatin binding subunit of the PBAF complex, but the molecular mechanism underlying this activity is not fully known. PBRM1 contains six tandem bromodomains which are known to cooperate in binding of nucleosomes acetylated at histone H3 lysine 14 (H3K14ac). Using H3K14Ac and PHF10 ChIP-seq, along with CLIP-seq in Caki2 renal cancer cells, we demonstrate here that the second and fourth bromodomains from PBRM1 also bind nucleic acids, selectively associating with double stranded RNA elements. Disruption of the RNA binding pocket is found to compromise PBRM1 chromatin binding and inhibit PBRM1-mediated cellular growth effects.

2023-02-24 | GSE221619 | GEO

PBRM1 bromodomains associate with RNA to facilitate chromatin association (ChIP-seq)

2023-02-24 | GSE221618 | GEO

PBRM1 bromodomains associate with RNA to facilitate chromatin association.

Project description:PBRM1 is a subunit of the PBAF chromatin remodeling complex, which is mutated in 40-50% of clear cell renal cell carcinoma patients. It is thought to largely function as a chromatin binding subunit of the PBAF complex, but the molecular mechanism underlying this activity is not fully known. PBRM1 contains six tandem bromodomains which are known to cooperate in binding of nucleosomes acetylated at histone H3 lysine 14 (H3K14ac). Here, we demonstrate that the second and fourth bromodomains from PBRM1 also bind nucleic acids, selectively associating with double stranded RNA elements. Disruption of the RNA binding pocket is found to compromise PBRM1 chromatin binding and inhibit PBRM1-mediated cellular growth effects.

| S-EPMC10164552 | biostudies-literature

PBRM1 bromodomains associate with RNA to facilitate chromatin association

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-02-24 | GSE221620 | GEO

Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci

Project description:This SuperSeries is composed of the following subset Series: GSE25597: Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci (ChIP-chip) GSE25598: Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci (expression) GSE25600: Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci (MNase) Refer to individual Series

2011-01-07 | E-GEOD-25605 | biostudies-arrayexpress

Genome-wide chromatin profiles of PBRM1 [RNA-Seq]

Project description:PBRM1 is an accessory subunit of the PBAF subclass of the SWI/SNF chromatin remodeler. The inactivation of PBRM1 is the second most frequent mutational event in kidney tumorigenesis. Here we show that in VHL-deficient ccRCC tumors, PBRM1 loss results in an altered PBAF complex that retains the association between SMARCA4 and ARID2 but disengages BRD7 from SMARCA4. The PBRM1-deficient PBAF complexes redistribute from promoter proxy regions to distal enhancer regions. The ATPase function of SMARCA4 enhances the recruitment of nuclear factor RELA to aberrant sites and promotes NF-κB activity. Proteasome inhibitor bortezomib reverses NF-κB activation by reducing RELA binding at regions bound by PBRM1-deficient PBAF and delays PBRM1-deficient tumor growth. In conclusion, PBRM1 safeguards the chromatin by repressing aberrant liberation of pro-tumorigenic NF-κB target genes by residual PBRM1-deficient PBAF complexes.

2023-02-13 | GSE152734 | GEO

Genome-wide chromatin profiles of PBRM1 [ChIP-Seq]

Project description:PBRM1 encodes an accessory subunit of the PBAF subclass of the SWI/SNF chromatin remodeler and the inactivation of PBRM1 is the second most frequent mutational event in kidney cancer. However, the impact of PBRM1 loss on chromatin remodeling, especially pertaining to kidney tumorigenesis, has not been well examined. Here we show that in VHL-deficient renal tumors, PBRM1 deficiency results in aberrant PBAF complexes that localize to de novo genomic loci and activate the pro-tumorigenic NF-?B pathway. PBRM1-deficient PBAF complexes, despite retaining the association between SMARCA4 and ARID2, have loosely tethered BRD7 and redistribute from promoter proximal regions to distal enhancers containing NF-?B motifs. Subsequently, PBRM1-deficient cells display heightened NF-?B activity in multiple models and clinical samples. The ATPase function of SMARCA4 maintains chromatin occupancy of both pre-existing and newly acquired RELA specific to PBRM1 loss, and activates downstream target gene expression. Proteasome inhibitor bortezomib reverses NF-?B activation by reducing RELA occupancy and delays growth of PBRM1-deficient tumors. In conclusion, PBRM1 safeguards the chromatin by repressing aberrant liberation of pro-tumorigenic NF-?B target genes by residual PBRM1-deficient PBAF complexes.

2023-02-13 | GSE152681 | GEO

PBRM1 Knockdown in RCC Cell Lines

Project description:PBRM1 was found to be mutated in a high percentage of clear cell RCCs. We performed knockdown of PBRM1 via siRNA and compared with scrambled control in three different RCC cell lines. PBRM1 siRNA and mock treated cell lines were normalized together with 'hypoxic' clear cell renal tumors and normal renal tissue samples from GSE17818.

2011-01-20 | E-GEOD-22316 | biostudies-arrayexpress

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