The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication

Hossein Davarinejad, Yi-Chun Huang, Benoit Mermaz, Chantal Leblanc, Axel Poulet, Geoffrey Thomson, Valentin Joly, Marcelo Muñoz, Alexis Arvanitis-Vigneault, Devisree Valsakumar, Gonzalo Villarino, Alex Ross, Benjamin H. Rotstein, Emilio I. Alarcon, Joseph S. Brunzelle, Philipp Voigt, Jie Dong, Jean-François Couture, Yannick Jacob

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The tail of replication-dependent histone H3.1 varies from that of replication-independent H3.3 at the amino acid located at position 31 in plants and animals, but no function has been assigned to this residue to demonstrate a unique and conserved role for H3.1 during replication. We found that TONSOKU (TSK/TONSL), which rescues broken replication forks, specifically interacts with H3.1 via recognition of alanine 31 by its tetratricopeptide repeat domain. Our results indicate that genomic instability in the absence of ATXR5/ATXR6-catalyzed histone H3 lysine 27 monomethylation in plants depends on H3.1, TSK, and DNA polymerase theta (Pol θ). This work reveals an H3.1-specific function during replication and a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and TSK, which relies on histone monomethyltransferases and reading of the H3.1 variant.
Original languageEnglish
Pages (from-to)1281-1286
Number of pages6
Issue number6586
Publication statusPublished - 17 Mar 2022


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