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Release of Histone H3K4-reading transcription factors from chromosomes in mitosis is independent of adjacent H3 phosphorylation

Lookup NU author(s): Rebecca Harris, Dr Maninder Heer, Dr Mark Levasseur, Dr Tyrell Cartwright, Beth Weston, Jennifer Mitchell, Dr Jonathan Coxhead, Dr Luke GaughanORCiD, Dr Lisa PrendergastORCiD, Professor Jonathan HigginsORCiD



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


© 2023, The Author(s). Histone modifications influence the recruitment of reader proteins to chromosomes to regulate events including transcription and cell division. The idea of a histone code, where combinations of modifications specify unique downstream functions, is widely accepted and can be demonstrated in vitro. For example, on synthetic peptides, phosphorylation of Histone H3 at threonine-3 (H3T3ph) prevents the binding of reader proteins that recognize trimethylation of the adjacent lysine-4 (H3K4me3), including the TAF3 component of TFIID. To study these combinatorial effects in cells, we analyzed the genome-wide distribution of H3T3ph and H3K4me2/3 during mitosis. We find that H3T3ph anti-correlates with adjacent H3K4me2/3 in cells, and that the PHD domain of TAF3 can bind H3K4me2/3 in isolated mitotic chromatin despite the presence of H3T3ph. Unlike in vitro, H3K4 readers are still displaced from chromosomes in mitosis in Haspin-depleted cells lacking H3T3ph. H3T3ph is therefore unlikely to be responsible for transcriptional downregulation during cell division.

Publication metadata

Author(s): Harris RJ, Heer M, Levasseur MD, Cartwright TN, Weston B, Mitchell JL, Coxhead JM, Gaughan L, Prendergast L, Rico D, Higgins JMG

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2023

Volume: 14

Online publication date: 09/11/2023

Acceptance date: 31/10/2023

Date deposited: 20/11/2023

ISSN (electronic): 2041-1723

Publisher: Springer Nature


DOI: 10.1038/s41467-023-43115-3


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Funder referenceFunder name
106951/Z/15/ZWellcome Trust
Barbour Foundation
J.G.W. Patterson Foundation
WM130089Royal Society