PXD039519-1

PXD039519 is an original dataset announced via ProteomeXchange.

Title	RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly
Description	In 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.
HostingRepository	PRIDE
AnnounceDate	2024-05-16
AnnouncementXML	Submission_2024-05-16_13:35:29.396.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Joao Paulo
SpeciesList	scientific name: Schizosaccharomyces pombe OY26; NCBI TaxID: 649908;
ModificationList	monohydroxylated residue
Instrument	Orbitrap Exploris 480; Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2023-01-17 01:29:51	ID requested
⏵ 1	2024-05-16 13:35:29	announced
2	2024-10-22 06:39:33	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: MTREC/NURS, long noncoding RNAs (lncRNA), H3K9 deacetylation, Clr3, H3K9 methylation, Clr4/SUV39H, heterochromatin nucleation, Sir2,De novo heterochromatin formation, nuclear exosome

Mo Motamedi
contact affiliation	Massachusetts General Hospital Center for Cancer Research and Department of Medicine Harvard Medical School Charlestown, MA, 02129, USA
contact email	mo_motamedi@hms.harvard.edu
lab head
Joao Paulo
contact affiliation	Harvard Medical School
contact email	joao_paulo@post.harvard.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD039519
     1. Label: PRIDE project
     2. Name: RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly