PXD018175-1

PXD018175 is an original dataset announced via ProteomeXchange.

Title	Complete loss of H3K9 methylation dissolves mouse heterochromatin organization
Description	Histone H3 lysine 9 (H3K9) methylation is a central epigenetic modification that defines heterochromatin from unicellular to multicellular organisms. In mammalian cells, H3K9 methylation can be catalyzed by at least six distinct SET domain enzymes: Suv39h1/Suv39h2, Eset1/Eset2 and G9a/Glp. We used mouse embryonic fibroblasts (MEFs) with a conditional mutation for Eset1 and introduced progressive deletions for the other SET domain genes by CRISPR/Cas9 technology. Compound mutant MEFs for all 6 SET domain methyltransferase (KMT) genes lack all H3K9 methylation states, derepress nearly all families of repeat elements and display genomic instabilities. Strikingly, the 6KO H3K9 KMT MEFs no longer maintain heterochromatin organization and have lost electron-dense heterochromatin. This is the first analysis of H3K9 methylation deficient mammalian chromatin and reveals a crucial function for H3K9 methylation in protecting heterochromatin organization and genome integrity.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:32:58.081.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Gerhard Mittler
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	asymmetric dimethyl-L-arginine; omega-N-methyl-L-arginine; N6-methyl-L-lysine; phosphorylated residue; N6-propanoyl-L-lysine; monohydroxylated residue; symmetric dimethyl-L-arginine; N6-acetyl-L-lysine; deamidated residue; N6,N6,N6-trimethyl-L-lysine; iodoacetamide derivatized residue; N6,N6-dimethyl-L-lysine
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2020-03-24 23:18:16	ID requested
⏵ 1	2024-10-07 13:32:58	announced

Montavon T, Shukeir N, Erikson G, Engist B, Onishi-Seebacher M, Ryan D, Musa Y, Mittler G, Meyer AG, Genoud C, Jenuwein T, Complete loss of H3K9 methylation dissolves mouse heterochromatin organization. Nat Commun, 12(1):4359(2021) [pubmed]

10.1038/s41467-021-24532-8;

submitter keyword: repeat silencing, heterochromatin organization, histone methyltransferases,Proteomic quantification of H3K9 methylation, genome stability

Gerhard Mittler
contact affiliation	Proteomics Unit - Research Facility Max Planck Institute of Immunobiology and Epigenetics Stübeweg 51 79108 Freiburg
contact email	mittler@ie-freiburg.mpg.de
lab head
Gerhard Mittler
contact affiliation	Proteomics Unit, Max Planck Institute of Immunobiology and Epigenetics
contact email	mittler@ie-freiburg.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD018175
     1. Label: PRIDE project
     2. Name: Complete loss of H3K9 methylation dissolves mouse heterochromatin organization