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RNA fine-tunes estrogen receptor-alpha binding on low-affinity DNA motifs for transcriptional regulation

ABSTRACT: RNA fine-tunes estrogen receptor-alpha binding on low-affinity DNA motifs for transcriptional regulation

PROVIDER: PRJNA1006735 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25690517.fastq.gz	Fastqsanger.gz
	SRR25690518_1.fastq.gz	Fastqsanger.gz
	SRR25690518_2.fastq.gz	Fastqsanger.gz
	SRR25690519_1.fastq.gz	Fastqsanger.gz
	SRR25690519_2.fastq.gz	Fastqsanger.gz

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RNA fine-tunes estrogen receptor-alpha binding on low-affinity DNA motifs for transcriptional regulation

Project description:Transcription factors (TFs) regulate gene expression by binding, with varying strength, to DNA via their DNA-binding domain. Additionally, some TFs also interact with RNA, which modulates transcription factor binding to chromatin. However, whether RNA-mediated TF binding results in differential transcriptional outcomes remains unknown. In this study, we demonstrate that estrogen receptor α (ERα), a ligand-activated TF, interacts with RNA in a ligand-dependent manner. Defects in RNA binding lead to genome-wide loss of ERα recruitment, particularly at weaker ERα-motifs. Furthermore, ERα mobility in the nucleus increases in the absence of its RNA-binding capacity. Unexpectedly, this increased mobility coincides with robust polymerase loading and transcription of ERα-regulated genes that harbor low-strength motifs. However, highly stable binding of ERα on chromatin negatively impacts ligand-dependent transcription. Collectively, our results suggest that RNA interactions spatially confine ERα on low-affinity sites to fine-tune gene transcription.

2024-09-06 | GSE241216 | GEO

RNA fine-tunes estrogen receptor-alpha binding on low-affinity DNA motifs for transcriptional regulation.

Project description:Transcription factors (TFs) regulate gene expression by binding with varying strengths to DNA via their DNA-binding domain. Additionally, some TFs also interact with RNA, which modulates transcription factor binding to chromatin. However, whether RNA-mediated TF binding results in differential transcriptional outcomes remains unknown. In this study, we demonstrate that estrogen receptor α (ERα), a ligand-activated TF, interacts with RNA in a ligand-dependent manner. Defects in RNA binding lead to genome-wide loss of ERα recruitment, particularly at weaker ERα-motifs. Furthermore, ERα mobility in the nucleus increases in the absence of its RNA-binding capacity. Unexpectedly, this increased mobility coincides with robust polymerase loading and transcription of ERα-regulated genes that harbor low-strength motifs. However, highly stable binding of ERα on chromatin negatively impacts ligand-dependent transcription. Collectively, our results suggest that RNA interactions spatially confine ERα on low-affinity sites to fine-tune gene transcription.

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