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PXD050442-1

PXD050442 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCytoplasmic DIS3 degrades circular RNAs independently of the exosome
DescriptionCircular 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.
HostingRepositoryPRIDE
AnnounceDate2025-05-05
AnnouncementXMLSubmission_2025-05-05_04:00:04.309.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD050442
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterAstrid Bruckmann
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListS-carboxamidoethyl-L-cysteine; deamidated residue; iodoacetamide derivatized residue
InstrumentmaXis
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-03-07 06:21:47ID requested
12025-05-05 04:00:04announced
Publication List
10.6019/PXD050442;
Keyword List
submitter keyword: exosome,circular RNAs, DIS3, degradation, circRNA
Contact List
Astrid Bruckmann
contact affiliationUniversity Regensburg, Biochemistry I,Mass spectrometry group
contact emailastrid.bruckmann@ur.de
lab head
Astrid Bruckmann
contact affiliationUniversity Regensburg
contact emailastrid.bruckmann@ur.de
dataset submitter
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Dataset FTP location
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