H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex. / Saredi, Giulia; Huang, Hongda; Hammond, Colin M; Alabert, Constance; Bekker-Jensen, Simon; Forne, Ignasi; Reverón-Gómez, Nazaret; Foster, Benjamin M; Mlejnkova, Lucie; Bartke, Till; Cejka, Petr; Mailand, Niels; Imhof, Axel; Patel, Dinshaw J; Groth, Anja.

In: Nature, Vol. 534, No. 7609, 30.06.2016, p. 714-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Saredi, G, Huang, H, Hammond, CM, Alabert, C, Bekker-Jensen, S, Forne, I, Reverón-Gómez, N, Foster, BM, Mlejnkova, L, Bartke, T, Cejka, P, Mailand, N, Imhof, A, Patel, DJ & Groth, A 2016, 'H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex', Nature, vol. 534, no. 7609, pp. 714-8. https://doi.org/10.1038/nature18312

APA

Saredi, G., Huang, H., Hammond, C. M., Alabert, C., Bekker-Jensen, S., Forne, I., Reverón-Gómez, N., Foster, B. M., Mlejnkova, L., Bartke, T., Cejka, P., Mailand, N., Imhof, A., Patel, D. J., & Groth, A. (2016). H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex. Nature, 534(7609), 714-8. https://doi.org/10.1038/nature18312

Vancouver

Saredi G, Huang H, Hammond CM, Alabert C, Bekker-Jensen S, Forne I et al. H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex. Nature. 2016 Jun 30;534(7609):714-8. https://doi.org/10.1038/nature18312

Author

Saredi, Giulia ; Huang, Hongda ; Hammond, Colin M ; Alabert, Constance ; Bekker-Jensen, Simon ; Forne, Ignasi ; Reverón-Gómez, Nazaret ; Foster, Benjamin M ; Mlejnkova, Lucie ; Bartke, Till ; Cejka, Petr ; Mailand, Niels ; Imhof, Axel ; Patel, Dinshaw J ; Groth, Anja. / H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex. In: Nature. 2016 ; Vol. 534, No. 7609. pp. 714-8.

Bibtex

@article{ef3285e4734e4d9f91d74ce6076a1a22,
title = "H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex",
abstract = "After DNA replication, chromosomal processes including DNA repair and transcription take place in the context of sister chromatids. While cell cycle regulation can guide these processes globally, mechanisms to distinguish pre- and post-replicative states locally remain unknown. Here we reveal that new histones incorporated during DNA replication provide a signature of post-replicative chromatin, read by the human TONSL–MMS22L homologous recombination complex. We identify the TONSL ankyrin repeat domain (ARD) as a reader of histone H4 tails unmethylated at K20 (H4K20me0), which are specific to new histones incorporated during DNA replication and mark post-replicative chromatin until the G2/M phase of the cell cycle. Accordingly, TONSL–MMS22L binds new histones H3–H4 both before and after incorporation into nucleosomes, remaining on replicated chromatin until late G2/M. H4K20me0 recognition is required for TONSL–MMS22L binding to chromatin and accumulation at challenged replication forks and DNA lesions. Consequently, TONSL ARD mutants are toxic, compromising genome stability, cell viability and resistance to replication stress. Together, these data reveal a histone-reader-based mechanism for recognizing the post-replicative state, offering a new angle to understand DNA repair with the potential for targeted cancer therapy.",
keywords = "Chromatin, DNA Repair, DNA Replication, DNA-Binding Proteins, Genomic Instability, Histones, Homologous Recombination, Humans, Lysine, Methylation, Models, Molecular, Molecular Chaperones, NF-kappa B, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Journal Article, Research Support, Non-U.S. Gov't",
author = "Giulia Saredi and Hongda Huang and Hammond, {Colin M} and Constance Alabert and Simon Bekker-Jensen and Ignasi Forne and Nazaret Rever{\'o}n-G{\'o}mez and Foster, {Benjamin M} and Lucie Mlejnkova and Till Bartke and Petr Cejka and Niels Mailand and Axel Imhof and Patel, {Dinshaw J} and Anja Groth",
year = "2016",
month = jun,
day = "30",
doi = "10.1038/nature18312",
language = "English",
volume = "534",
pages = "714--8",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "7609",

}

RIS

TY - JOUR

T1 - H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex

AU - Saredi, Giulia

AU - Huang, Hongda

AU - Hammond, Colin M

AU - Alabert, Constance

AU - Bekker-Jensen, Simon

AU - Forne, Ignasi

AU - Reverón-Gómez, Nazaret

AU - Foster, Benjamin M

AU - Mlejnkova, Lucie

AU - Bartke, Till

AU - Cejka, Petr

AU - Mailand, Niels

AU - Imhof, Axel

AU - Patel, Dinshaw J

AU - Groth, Anja

PY - 2016/6/30

Y1 - 2016/6/30

N2 - After DNA replication, chromosomal processes including DNA repair and transcription take place in the context of sister chromatids. While cell cycle regulation can guide these processes globally, mechanisms to distinguish pre- and post-replicative states locally remain unknown. Here we reveal that new histones incorporated during DNA replication provide a signature of post-replicative chromatin, read by the human TONSL–MMS22L homologous recombination complex. We identify the TONSL ankyrin repeat domain (ARD) as a reader of histone H4 tails unmethylated at K20 (H4K20me0), which are specific to new histones incorporated during DNA replication and mark post-replicative chromatin until the G2/M phase of the cell cycle. Accordingly, TONSL–MMS22L binds new histones H3–H4 both before and after incorporation into nucleosomes, remaining on replicated chromatin until late G2/M. H4K20me0 recognition is required for TONSL–MMS22L binding to chromatin and accumulation at challenged replication forks and DNA lesions. Consequently, TONSL ARD mutants are toxic, compromising genome stability, cell viability and resistance to replication stress. Together, these data reveal a histone-reader-based mechanism for recognizing the post-replicative state, offering a new angle to understand DNA repair with the potential for targeted cancer therapy.

AB - After DNA replication, chromosomal processes including DNA repair and transcription take place in the context of sister chromatids. While cell cycle regulation can guide these processes globally, mechanisms to distinguish pre- and post-replicative states locally remain unknown. Here we reveal that new histones incorporated during DNA replication provide a signature of post-replicative chromatin, read by the human TONSL–MMS22L homologous recombination complex. We identify the TONSL ankyrin repeat domain (ARD) as a reader of histone H4 tails unmethylated at K20 (H4K20me0), which are specific to new histones incorporated during DNA replication and mark post-replicative chromatin until the G2/M phase of the cell cycle. Accordingly, TONSL–MMS22L binds new histones H3–H4 both before and after incorporation into nucleosomes, remaining on replicated chromatin until late G2/M. H4K20me0 recognition is required for TONSL–MMS22L binding to chromatin and accumulation at challenged replication forks and DNA lesions. Consequently, TONSL ARD mutants are toxic, compromising genome stability, cell viability and resistance to replication stress. Together, these data reveal a histone-reader-based mechanism for recognizing the post-replicative state, offering a new angle to understand DNA repair with the potential for targeted cancer therapy.

KW - Chromatin

KW - DNA Repair

KW - DNA Replication

KW - DNA-Binding Proteins

KW - Genomic Instability

KW - Histones

KW - Homologous Recombination

KW - Humans

KW - Lysine

KW - Methylation

KW - Models, Molecular

KW - Molecular Chaperones

KW - NF-kappa B

KW - Nuclear Proteins

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/nature18312

DO - 10.1038/nature18312

M3 - Journal article

C2 - 27338793

VL - 534

SP - 714

EP - 718

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7609

ER -

ID: 165693562