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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 möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Posttranslational Modification; Crystal-structure; Histone H3.3; Proteoform; Chromatin; Reveals
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Zeitschrift Molecular Cell
Quellenangaben Band: 85, Heft: 19, Seiten: 3554-3561 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Functional Epigenetics (IFE)