PXD050442 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Cytoplasmic DIS3 degrades circular RNAs independently of the exosome |
Description | Circular RNAs (circRNAs) are frequently generated during splicing. Their physiological roles, however, remain largely elusive. Some specific circRNAs function as microRNA (miRNA) or RNA binding protein (RBP) sponges or encode for proteins and are actively translated. Due to the lack of accessible ends, circRNAs are resistant to exonucleolytic cleavage and thus are more stable than linear RNAs. Nevertheless, circRNAs are most likely turned over by cellular degradation pathways. Here, we used a biochemical purification strategy to find nucleases that could degrade circRNAs. We identified the exosome-associated nuclease DIS3, which contains an endonucleolytic PIN domain and an exonuclease domain. We show that DIS3 can degrade circRNAs independently of the exosome in vitro. Although moderately, RNA-seq reveals that selected circRNAs are stabilized when DIS3 is reduced in vivo. Based on our data, we propose a model, in which cytoplasmic DIS3 contributes to the turnover of circRNAs in human cells. |
HostingRepository | PRIDE |
AnnounceDate | 2025-05-05 |
AnnouncementXML | Submission_2025-05-05_04:00:04.309.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD050442 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Astrid Bruckmann |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | S-carboxamidoethyl-L-cysteine; deamidated residue; iodoacetamide derivatized residue |
Instrument | maXis |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-03-07 06:21:47 | ID requested | |
⏵ 1 | 2025-05-05 04:00:04 | announced | |
Publication List
Keyword List
submitter keyword: exosome,circular RNAs, DIS3, degradation, circRNA |
Contact List
Astrid Bruckmann |
contact affiliation | University Regensburg, Biochemistry I,Mass spectrometry group |
contact email | astrid.bruckmann@ur.de |
lab head | |
Astrid Bruckmann |
contact affiliation | University Regensburg |
contact email | astrid.bruckmann@ur.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD050442
- Label: PRIDE project
- Name: Cytoplasmic DIS3 degrades circular RNAs independently of the exosome