PXD020686

PXD020686 is an original dataset announced via ProteomeXchange.

Title	The functional interactome of site-specifically ubiquitylated linker histone H1
Description	Decoding 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 demonstrate that site-specific ubiquitylation is a general functional regulator for linker histone H1.
HostingRepository	PRIDE
AnnounceDate	2021-07-20
AnnouncementXML	Submission_2021-07-19_23:58:53.027.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Florian Stengel
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitination signature dipeptidyl lysine; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	micrOTOF II; Q Exactive; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2020-08-02 23:03:47	ID requested
⏵ 1	2021-07-19 23:58:53	announced

H, ö, llm, ü, ller E, Geigges S, Niedermeier ML, Kammer KM, Kienle SM, R, ö, sner D, Scheffner M, Marx A, Stengel F, Site-specific ubiquitylation acts as a regulator of linker histone H1. Nat Commun, 12(1):3497(2021) [pubmed]

submitter keyword: linker histone H1, ubiquitin, posttranslational modification (PTM), chromatin, histone code, epigenetics

Florian Stengel
contact affiliation	Department of Biology – Cellular Proteostasis and Mass Spectrometry, University of Konstanz
contact email	florian.stengel@uni-konstanz.de
lab head
Florian Stengel
contact affiliation	Universität Konstanz
contact email	florian.stengel@uni-konstanz.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/07/PXD020686

PRIDE project URI

• PRIDE
  1. PXD020686
     1. Label: PRIDE project
     2. Name: The functional interactome of site-specifically ubiquitylated linker histone H1