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PXD025258-1

PXD025258 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSite-specific ubiquitylation acts as a regulator of linker histone H1
DescriptionDecoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. While this process is well studied for core histones and many of their PTMs, this is not the case for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the generation of site-specifically mono-ubiquitylated H1.2 via click chemistry and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that the H1 interactome is generally modulated by ubiquitylation and that site-specific ubiquitylation results in overlapping, but distinct interactomes. We further demonstrate that site-specific ubiquitylation of H1 affects the interaction with enzymes relevant for deubiquitylation and deacetylation. We finally show that site-specific ubiquitylation at position K64 impacts H1-dependent chromatosome assembly as well as H1-induced phase separation. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.
HostingRepositoryPRIDE
AnnounceDate2021-09-14
AnnouncementXMLSubmission_2021-09-14_08:16:56.604.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFlorian Stengel
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListmonomethylated residue; ubiquitinylated lysine; phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentmicrOTOF II; Orbitrap Fusion; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-04-08 04:11:09ID requested
12021-09-14 08:16:57announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: linker histone H1, ubiquitin, posttranslational modification (PTM), chromatin, histone code, epigenetics
Contact List
Florian Stengel
contact affiliationDepartment of Biology – Cellular Proteostasis and Mass Spectrometry, University of Konstanz
contact emailflorian.stengel@uni-konstanz.de
lab head
Florian Stengel
contact affiliationUniversität Konstanz
contact emailflorian.stengel@uni-konstanz.de
dataset submitter
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Dataset FTP location
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