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The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE197474 | GEO | 2025/02/14

REPOSITORIES: GEO

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The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.

Project description:The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.The role of DGCR8 in RNA processing in human embryonic teratocarcinoma PA-1 cells.

| PRJNA810443 | ENA

Effect of DGCR8 heterozygosity on steady state RNA levels in embryonic teratocarcinoma PA-1 cells

Project description:In this dataset we use total RNA-seq to study the effect of DGCR8 heterozygosity on steady state RNA levels

2025-02-14 | GSE197472 | GEO

Effect of DGCR8 heterozygosity on steady state miRNA levels in embryonic teratocarcinoma PA-1 cells

Project description:In this dataset we use small RNA-seq to study the effect of DGCR8 heterozygosity on steady state miRNA levels

2025-02-14 | GSE197470 | GEO

Effect of DGCR8 heterozygosity on steady state RNA levels in embryonic teratocarcinoma PA-1 cells

Project description:Effect of DGCR8 heterozygosity on steady state RNA levels in embryonic teratocarcinoma PA-1 cells

| PRJNA810447 | ENA

Effect of DGCR8 knockout and heterozygosity pri-miRNA processing in PA-1 cells

Project description:In this dataset we extract and sequence chromatin-associated RNA to study the effect of DGCR8 knockout and heterozygosity on pri-miRNA processing

2025-02-14 | GSE197469 | GEO

DGCR8 Mediates Repair of UV-Induced DNA Damage Independently of RNA Processing.

Project description:Ultraviolet (UV) radiation is a carcinogen that generates DNA lesions. Here, we demonstrate an unexpected role for DGCR8, an RNA binding protein that canonically functions with Drosha to mediate microRNA processing, in the repair of UV-induced DNA lesions. Treatment with UV induced phosphorylation on serine 153 (S153) of DGCR8 in both human and murine cells. S153 phosphorylation was critical for cellular resistance to UV, the removal of UV-induced DNA lesions, and the recovery of RNA synthesis after UV exposure but not for microRNA expression. The RNA-binding and Drosha-binding activities of DGCR8 were not critical for UV resistance. DGCR8 depletion was epistatic to defects in XPA, CSA, and CSB for UV sensitivity. DGCR8 physically interacted with CSB and RNA polymerase II. JNKs were involved in the UV-induced S153 phosphorylation. These findings suggest that UV-induced S153 phosphorylation mediates transcription-coupled nucleotide excision repair of UV-induced DNA lesions in a manner independent of microRNA processing.

| S-EPMC5423785 | biostudies-literature

Effect of DGCR8 heterozygosity on steady state miRNA levels in embryonic teratocarcinoma PA-1 cells

Project description:Effect of DGCR8 heterozygosity on steady state miRNA levels in embryonic teratocarcinoma PA-1 cells

| PRJNA810448 | ENA

Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing.

Project description:The RNA-binding protein DiGeorge Critical Region 8 (DGCR8) and its partner nuclease Drosha are essential for processing of microRNA (miRNA) primary transcripts (pri-miRNAs) in animals. Previous work showed that DGCR8 forms a highly stable and active complex with ferric [Fe(III)] heme using two endogenous cysteines as axial ligands. Here we report that reduction of the heme iron to the ferrous [Fe(II)] state in DGCR8 abolishes the pri-miRNA processing activity. The reduction causes a dramatic increase in the rate of heme dissociation from DGCR8, rendering the complex labile. Electronic absorption, magnetic circular dichroism, and resonance Raman spectroscopies indicate that reduction of the heme iron is accompanied by loss of the cysteines as axial ligands. ApoDGCR8 dimers, generated through reduction and removal of the heme, show low levels of activity in pri-miRNA processing in vitro. Importantly, ferric, but not ferrous, heme restores the activity of apoDGCR8 to the level of the native ferric complex. This study demonstrates binding specificity of DGCR8 for ferric heme, provides direct biochemical evidence for ferric heme serving as an activator for miRNA maturation, and suggests that an intracellular environment increasing the availability of ferric heme may enhance the efficiency of pri-miRNA processing.

| S-EPMC3277547 | biostudies-literature

DGCR8-dependent efficient pri-miRNA processing of human pri-miR-9-2.

Project description:Microprocessor complex, including DiGeorge syndrome critical region gene 8 (DGCR8) and DROSHA, recognizes and cleaves primary transcripts of microRNAs (pri-miRNAs) in the maturation of canonical miRNAs. The study of DGCR8 haploinsufficiency reveals that the efficiency of this activity varies for different miRNA species. It is thought that this variation might be associated with the risk of schizophrenia with 22q11 deletion syndrome caused by disruption of the DGCR8 gene. However, the underlying mechanism for varying action of DGCR8 with each miRNA remains largely unknown. Here, we used in vivo monitoring to measure the efficiency of DGCR8-dependent microprocessor activity in cultured cells. We confirmed that this system recapitulates the microprocessor activity of endogenous pri-miRNA with expression of a ratiometric fluorescence reporter. Using this system, we detected mir-9-2 as one of the most efficient targets. We also identified a novel DGCR8-responsive RNA element, which is highly conserved among mammalian species and could be regulated at epi-transcriptome (RNA modification) level. This unique feature between DGCR8 and pri-miR-9-2 processing may suggest a link to the risk of schizophrenia.

| S-EPMC7995608 | biostudies-literature

Elucidating the Role of Microprocessor Protein DGCR8 in Bending RNA Structures.

Project description:Although conformational dynamics of RNA molecules are potentially important in microRNA (miRNA) processing, the role of the protein binding partners in facilitating the requisite structural changes is not well understood. In previous work, we and others have demonstrated that nonduplex structural elements and the conformational flexibility they support are necessary for efficient RNA binding and cleavage by the proteins associated with the two major stages of miRNA processing. However, recent studies showed that the protein DGCR8 binds primary miRNA and duplex RNA with similar affinities. Here, we study RNA binding by a small recombinant construct of the DGCR8 protein and the RNA conformation changes that result. This construct, the DGCR8 core, contains two double-stranded RNA-binding domains (dsRBDs) and a C-terminal tail. To assess conformational changes resulting from binding, we applied small-angle x-ray scattering with contrast variation to detect conformational changes of primary-miR-16-1 in complex with the DGCR8 core. This method reports only on the RNA conformation within the complex and suggests that the protein bends the RNA upon binding. Supporting work using smFRET to study the conformation of RNA duplexes bound to the core also shows bending. Together, these studies elucidate the role of DGCR8 in interacting with RNA during the early stages of miRNA processing.

| S-EPMC7822732 | biostudies-literature

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