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Article

Histone H2A ubiquitination does not preclude histone H1 binding, but it facilitates its association with the nucleosome.

The Journal of biological chemistry - 11 Feb 2005

Jason Laure J M, Finn Ron M, Lindsey George, Ausió Juan

Abstract excerpt

Histone H2A ubiquitination is a bulky posttranslational modification that occurs at the vicinity of the binding site for linker histones in the nucleosome. Therefore, we took several experimental approaches to investigate the role of ubiquitinated H2A (uH2A) in the binding of linker histones. Our results showed that uH2A was present in situ in histone H1-containing nucleosomes. Notably in vitro experiments using...

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PMID: 15546875
DOI: 10.1074/jbc.M410203200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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