PuSH - Publication Server of Helmholtz Zentrum München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Keogh, M.C.* ; Almouzni, G.* ; Andrews, A.J.* ; Armache, K.J.* ; Arrowsmith, C.H.* ; Baek, S.H.* ; Bedford, M.T.* ; Bernstein, E.* ; Côté, J.-A.* ; David, Y.* ; Denu, J.M.* ; Fierz, B.* ; Garcia, B.A.* ; Glass, K.C.* ; Gozani, O.* ; Helin, K.* ; Henikoff, S.* ; Jensen, O.N.* ; Josefowicz, S.Z.* ; Kelleher, N.L.* ; Kutateladze, T.G.* ; Lindner, H.H.* ; Lu, C.* ; Luger, K.* ; Mallick, P.* ; Musselman, C.A.* ; Muir, T.W.* ; Pasa-Tolic, L.* ; Schneider, R. ; Shi, X.* ; Shi, Y.* ; Sidoli, S.* ; Smith, L.M.* ; Tyler, J.K.* ; Wolberger, C.* ; Workman, J.L.* ; Strahl, B.D.* ; Young, N.L.*

A needed nomenclature for nucleosomes.

Mol. Cell 85, 3554-3561 (2025)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.
Impact Factor
Scopus SNIP
Altmetric
16.600
2.895
Tags
Annotations
Special Publikation
Hide on homepage

Edit extra information
Edit own tags
Private
Edit own annotation
Private
Hide on publication lists
on hompage
Mark as special
publikation
Publication type Article: Journal article
Document type Review
Keywords Posttranslational Modification; Crystal-structure; Histone H3.3; Proteoform; Chromatin; Reveals
Language english
Publication Year 2025
HGF-reported in Year 2025
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Journal Molecular Cell
Quellenangaben Volume: 85, Issue: 19, Pages: 3554-3561 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status Peer reviewed
Institute(s) Institute of Functional Epigenetics (IFE)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Helmholtz Diabetes Center
PSP Element(s) G-502800-001
DOI 10.1016/j.molcel.2025.08.029
WOS ID 001589254400001
Scopus ID 105017234334
PubMed ID 41043390
Erfassungsdatum 2025-10-16
[➜Report correction]