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PXD039519

PXD039519 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleRNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly
DescriptionIn eukaryotes, the Suv39 family of proteins tri-methylate lysine 9 of histone H3 (H3K9me) to form constitutive heterochromatin. However, how Suv39 proteins are nucleated at heterochromatin is not fully described. In the fission yeast, current models posit that Argonaute1-associated small RNAs (sRNAs) nucleate the sole H3K9 methyltransferase, Clr4/SUV39H, to centromeres. Here, we show that in the absence of all sRNAs and H3K9me, the Mtl1 and Red1 core (MTREC)/PAXT complex nucleates Clr4/SUV39H at a heterochromatic long noncoding RNA (lncRNA) at which the two H3K9 deacetylases, Sir2 and Clr3, also accumulate by distinct mechanisms. Iterative cycles of H3K9 deacetylation and methylation spread Clr4/SUV39H from the nucleation center in an sRNA-independent manner, generating a basal H3K9me state. This is acted upon by the RNAi machinery to augment and amplify the Clr4/H3K9me signal at centromeres to establish heterochromatin. Overall, our data reveal that lncRNAs and RNA quality control factors can nucleate heterochromatin and function as epigenetic silencers in eukaryotes.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_06:39:33.241.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJoao Paulo
SpeciesList scientific name: Schizosaccharomyces pombe OY26; NCBI TaxID: 649908;
ModificationListmonohydroxylated residue
InstrumentOrbitrap Exploris 480; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-01-17 01:29:51ID requested
12024-05-16 13:35:29announced
22024-10-22 06:39:33announced2024-10-22: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: MTREC/NURS, long noncoding RNAs (lncRNA), H3K9 deacetylation, Clr3, H3K9 methylation, Clr4/SUV39H, heterochromatin nucleation, Sir2,De novo heterochromatin formation, nuclear exosome
Contact List
Mo Motamedi
contact affiliationMassachusetts General Hospital Center for Cancer Research and Department of Medicine Harvard Medical School Charlestown, MA, 02129, USA
contact emailmo_motamedi@hms.harvard.edu
lab head
Joao Paulo
contact affiliationHarvard Medical School
contact emailjoao_paulo@post.harvard.edu
dataset submitter
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Dataset FTP location
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