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

Rebecca J. Harris, Maninder Heer, Mark D. Levasseur, Tyrell N. Cartwright, Bethany Weston, Jennifer L. Mitchell, Jonathan M. Coxhead, Luke Gaughan, Lisa Prendergast, Daniel Rico () and Jonathan M. G. Higgins ()
Additional contact information
Rebecca J. Harris: Newcastle University
Maninder Heer: Newcastle University
Mark D. Levasseur: Newcastle University
Tyrell N. Cartwright: Newcastle University
Bethany Weston: Newcastle University
Jennifer L. Mitchell: Newcastle University
Jonathan M. Coxhead: Newcastle University
Luke Gaughan: Newcastle University
Lisa Prendergast: Newcastle University
Daniel Rico: Newcastle University
Jonathan M. G. Higgins: Newcastle University

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract 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.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-43115-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43115-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-43115-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().