The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication-Reference-Cited by-同舟云学术

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

Published:2022-03-18 Issue:6586 Volume:375 Page:1281-1286
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Davarinejad Hossein¹^ORCID,Huang Yi-Chun²^ORCID,Mermaz Benoit²^ORCID,LeBlanc Chantal²^ORCID,Poulet Axel²^ORCID,Thomson Geoffrey²^ORCID,Joly Valentin²^ORCID,Muñoz Marcelo³⁴^ORCID,Arvanitis-Vigneault Alexis¹^ORCID,Valsakumar Devisree⁵⁶^ORCID,Villarino Gonzalo²^ORCID,Ross Alex³⁴^ORCID,Rotstein Benjamin H.⁴⁷^ORCID,Alarcon Emilio I.³⁴,Brunzelle Joseph S.⁸^ORCID,Voigt Philipp⁵⁶^ORCID,Dong Jie²⁹^ORCID,Couture Jean-François¹^ORCID,Jacob Yannick²^ORCID

Affiliation:

1. Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada.

2. Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06511, USA.

3. Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.

4. Epigenetics Programme, Babraham Institute, Cambridge CB22 3AT, UK.

5. BEaTS Research Laboratory, Division of Cardiac Surgery, University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7, Canada.

6. Department of Biochemistry, Microbiology, and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada.

7. University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7, Canada.

8. Department of Molecular Pharmacology and Biological Chemistry, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

9. Institute of Crop Science, Zhejiang University, Hangzhou 310058, China.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference64 articles.

1. Identification of the MMS22L-TONSL Complex that Promotes Homologous Recombination

2. The Histone Chaperones ASF1 and CAF-1 Promote MMS22L-TONSL-Mediated Rad51 Loading onto ssDNA during Homologous Recombination in Human Cells

3. A Genome-wide Camptothecin Sensitivity Screen Identifies a Mammalian MMS22L-NFKBIL2 Complex Required for Genomic Stability

4. The MMS22L-TONSL Complex Mediates Recovery from Replication Stress and Homologous Recombination

5. The MMS22L–TONSL heterodimer directly promotes RAD51‐dependent recombination upon replication stress

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