RIF1 coordinates the stepwise post-replicative H3K9me3 recovery
Abstract
DNA replication dilutes parental histones and their post-translational modifications, requiring restoration of epigenetic marks on newly incorporated histones. H3K9me3 restoration is unusually slow, extending into the following G1 phase, but the mechanisms governing this delay remain unclear. Here, we show that RIF1 reassociation with heterochromatin during mitotic exit establishes a permissive chromatin environment for histone methyltransferases to resume H3K9me3 deposition. RIF1 promotes recruitment of SUV39H1 and HP1α/β and the increase of H3K9 tri-methylation during G1. RIF1 also recruits protein phosphatase 1α (PP1α) to heterochromatin, and RIF1-PP1α interaction is essential for the maintenance of H3K9me3 levels. Moreover, RIF1-PP1 complex temporally restrains the activity of Aurora kinase at heterochromatin, preventing premature H3S10 phosphorylation before replication and creating a permissive time-window for SUV39H-mediated reinstatement of H3K9me3.
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BibTeX
@article{chen2026rif1,
title = {{RIF1 coordinates the stepwise post-replicative H3K9me3 recovery}},
author = {Naiming Chen and Susanne Bandau and Reshma Ravindran Nair and Bram Prevo and Takayo Sasaki and Shaun Webb and Simone di Sanzo and Hao Jiang and David Shapira and Sophia Lipattsev and Jose de las Heras and Moritz Voelker-Albert and Angus Lamond and David M. Gilbert and Constance Alabert and Sara C.B. Buonomo},
journal = {Cell Reports},
year = {2026},
month = oct,
doi = {10.1016/j.celrep.2026.118191},
url = {https://linkinghub.elsevier.com/retrieve/pii/S2211124726012702},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - RIF1 coordinates the stepwise post-replicative H3K9me3 recovery
AU - Naiming Chen
AU - Susanne Bandau
AU - Reshma Ravindran Nair
AU - Bram Prevo
AU - Takayo Sasaki
AU - Shaun Webb
AU - Simone di Sanzo
AU - Hao Jiang
AU - David Shapira
AU - Sophia Lipattsev
AU - Jose de las Heras
AU - Moritz Voelker-Albert
AU - Angus Lamond
AU - David M. Gilbert
AU - Constance Alabert
AU - Sara C.B. Buonomo
PY - 2026
DA - 2026/10/30
JO - Cell Reports
DO - 10.1016/j.celrep.2026.118191
UR - https://linkinghub.elsevier.com/retrieve/pii/S2211124726012702
AB - DNA replication dilutes parental histones and their post-translational modifications, requiring restoration of epigenetic marks on newly incorporated histones. H3K9me3 restoration is unusually slow, extending into the following G1 phase, but the mechanisms governing this delay remain unclear. Here, we show that RIF1 reassociation with heterochromatin during mitotic exit establishes a permissive chromatin environment for histone methyltransferases to resume H3K9me3 deposition. RIF1 promotes recruitment of SUV39H1 and HP1α/β and the increase of H3K9 tri-methylation during G1. RIF1 also recruits protein phosphatase 1α (PP1α) to heterochromatin, and RIF1-PP1α interaction is essential for the maintenance of H3K9me3 levels. Moreover, RIF1-PP1 complex temporally restrains the activity of Aurora kinase at heterochromatin, preventing premature H3S10 phosphorylation before replication and creating a permissive time-window for SUV39H-mediated reinstatement of H3K9me3.
SN - 2211-1247
ER -