Faculty, Staff and Student Publications

Language

English

Publication Date

10-2-2025

Journal

Molecular Cell: Cell Press

DOI

10.1016/j.molcel.2025.08.029

PMID

41043390

PMCID

PMC12778995

PubMedCentral® Posted Date

1-8-2026

PubMedCentral® Full Text Version

Author MSS

Abstract

Histone post-translational modifications (PTMs) are crucial to eukaryotic genome regulation, with a range of reported functions and mechanisms of action. Though often studied individually, it has long been recognized that the modifications function by combinatorial synergy or antagonism. Interplay may involve PTMs on the same histone, within the same nucleosome (containing a histone octamer), or between nucleosomes in higher-order chromatin. Given this, the field must distinguish ever greater complexity, and the context in which it is studied, with brevity and precision. The proteoform was introduced to define individual forms of a protein by sequence and PTMs, followed by the nucleoform to describe the particular gathering of histones within an individual nucleosome. There is now a need to define specific forms of these entities in prose while providing space for experimental nuance. To this end, we introduce a nomenclature that can express discrete PTMs, proteoforms, nucleoforms, or situations where defined PTMs exist in an uncertain context. Though specifically designed for the chromatin field, adaptions of the framework could be used to describe-and thus dissect-how proteoforms are configured in functionally distinct complexes across biology.

Keywords

Nucleosomes, Protein Processing, Post-Translational, Histones, Humans, Terminology as Topic, Animals, Chromatin, Chromatin Assembly and Disassembly

Published Open-Access

yes

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