TY - JOUR
T1 - The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication
AU - Davarinejad, Hossein
AU - Huang, Yi-Chun
AU - Mermaz, Benoit
AU - Leblanc, Chantal
AU - Poulet, Axel
AU - Thomson, Geoffrey
AU - Joly, Valentin
AU - Muñoz, Marcelo
AU - Arvanitis-Vigneault, Alexis
AU - Valsakumar, Devisree
AU - Villarino, Gonzalo
AU - Ross, Alex
AU - Rotstein, Benjamin H.
AU - Alarcon, Emilio I.
AU - Brunzelle, Joseph S.
AU - Voigt, Philipp
AU - Dong, Jie
AU - Couture, Jean-François
AU - Jacob, Yannick
N1 - Funding Information:
Supported by NIH grant R35GM128661 (Y.J.), grants from the Natural Science Engineering Research Council and the Canadian Institutes of Health Research (PJG-47391S) (J.-F.C.), an Ontario Graduate Scholarship and a University of Ottawa Excellence Scholarship (H.D.), a Yale University Brown Fellowship (B.M.), Fonds de Recherche du Québec–Nature et Technologies (FRQNT) grant 272565 (V.J.), and a Strategic Research Postdoctoral Fellowship from the University of Ottawa Heart Institute and the Strategic Research Endowed Funds (M.M.). Work in the Voigt lab was supported by Wellcome Trust grant 104175/Z/14/Z Sir Henry Dale Fellowship (P.V.) and UK Biotechnology and Biological Sciences Research Council grant BBS/E/B/000C0421. The Wellcome Centre for Cell Biology received core funding from Wellcome Trust grant 203149. The EPPF was supported by the Wellcome Trust through Multi-User Equipment grant 101527/Z/13/Z. B.H.R. and E.I.A. thank NSERCRTI (RTI-2019-00009).
Publisher Copyright:
© 2022 American Association for the Advancement of Science. All rights reserved.
PY - 2022/3/17
Y1 - 2022/3/17
N2 - 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.
AB - 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.
U2 - 10.1126/science.abm5320
DO - 10.1126/science.abm5320
M3 - Article
SN - 0036-8075
VL - 375
SP - 1281
EP - 1286
JO - Science
JF - Science
IS - 6586
ER -