Site-specific ubiquitylation acts as a regulator of linker histone H1

Eva Höllmüller, Simon Geigges, Marie L. Niedermeier, Kai-Michael Kammer, Simon M. Kienle, Daniel Rösner, Martin Scheffner (), Andreas Marx () and Florian Stengel ()
Additional contact information
Eva Höllmüller: University of Konstanz
Simon Geigges: University of Konstanz
Marie L. Niedermeier: University of Konstanz
Kai-Michael Kammer: University of Konstanz
Simon M. Kienle: University of Konstanz
Daniel Rösner: University of Konstanz
Martin Scheffner: University of Konstanz
Andreas Marx: University of Konstanz
Florian Stengel: University of Konstanz

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract Decoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. This is well studied for PTMs of core histones but not for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the chemical synthesis of site-specifically mono-ubiquitylated H1.2 and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that site-specific ubiquitylation of H1 at position K64 modulates interactions with deubiquitylating enzymes and the deacetylase SIRT1. Moreover, it affects H1-dependent chromatosome assembly and phase separation resulting in a more open chromatosome conformation generally associated with a transcriptionally active chromatin state. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.

Date: 2021
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-021-23636-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23636-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-23636-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().