Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3

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

Standard

Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3. / Richards, Frederick; Llorca-Cardenosa, Marta J.; Langton, Jamie; Buch-Larsen, Sara C.; Shamkhi, Noor F.; Sharma, Abhishek Bharadwaj; Nielsen, Michael L.; Lakin, Nicholas D.

In: Nature Communications, Vol. 14, No. 1, 4310, 2023.

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

Harvard

Richards, F, Llorca-Cardenosa, MJ, Langton, J, Buch-Larsen, SC, Shamkhi, NF, Sharma, AB, Nielsen, ML & Lakin, ND 2023, 'Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3', Nature Communications, vol. 14, no. 1, 4310. https://doi.org/10.1038/s41467-023-40071-w

APA

Richards, F., Llorca-Cardenosa, M. J., Langton, J., Buch-Larsen, S. C., Shamkhi, N. F., Sharma, A. B., Nielsen, M. L., & Lakin, N. D. (2023). Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3. Nature Communications, 14(1), [4310]. https://doi.org/10.1038/s41467-023-40071-w

Vancouver

Richards F, Llorca-Cardenosa MJ, Langton J, Buch-Larsen SC, Shamkhi NF, Sharma AB et al. Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3. Nature Communications. 2023;14(1). 4310. https://doi.org/10.1038/s41467-023-40071-w

Author

Richards, Frederick ; Llorca-Cardenosa, Marta J. ; Langton, Jamie ; Buch-Larsen, Sara C. ; Shamkhi, Noor F. ; Sharma, Abhishek Bharadwaj ; Nielsen, Michael L. ; Lakin, Nicholas D. / Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3. In: Nature Communications. 2023 ; Vol. 14, No. 1.

Bibtex

@article{a33c16c2aa1a4a4592b69d957b533067,
title = "Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3",
abstract = "Although Poly(ADP-ribose)-polymerases (PARPs) are key regulators of genome stability, how site-specific ADP-ribosylation regulates DNA repair is unclear. Here, we describe a novel role for PARP1 and PARP2 in regulating Rad52-dependent replication fork repair to maintain cell viability when homologous recombination is dysfunctional, suppress replication-associated DNA damage, and maintain genome stability. Mechanistically, Mre11 and ATM are required for induction of PARP activity in response to replication stress that in turn promotes break-induced replication (BIR) through assembly of Rad52 at stalled/damaged replication forks. Further, by mapping ADP-ribosylation sites induced upon replication stress, we identify that PolD3 is a target for PARP1/PARP2 and that its site-specific ADP-ribosylation is required for BIR activity, replication fork recovery and genome stability. Overall, these data identify a critical role for Mre11-dependent PARP activation and site-specific ADP-ribosylation in regulating BIR to maintain genome integrity during DNA synthesis.",
author = "Frederick Richards and Llorca-Cardenosa, {Marta J.} and Jamie Langton and Buch-Larsen, {Sara C.} and Shamkhi, {Noor F.} and Sharma, {Abhishek Bharadwaj} and Nielsen, {Michael L.} and Lakin, {Nicholas D.}",
note = "Publisher Copyright: {\textcopyright} 2023, The Author(s).",
year = "2023",
doi = "10.1038/s41467-023-40071-w",
language = "English",
volume = "14",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3

AU - Richards, Frederick

AU - Llorca-Cardenosa, Marta J.

AU - Langton, Jamie

AU - Buch-Larsen, Sara C.

AU - Shamkhi, Noor F.

AU - Sharma, Abhishek Bharadwaj

AU - Nielsen, Michael L.

AU - Lakin, Nicholas D.

N1 - Publisher Copyright: © 2023, The Author(s).

PY - 2023

Y1 - 2023

N2 - Although Poly(ADP-ribose)-polymerases (PARPs) are key regulators of genome stability, how site-specific ADP-ribosylation regulates DNA repair is unclear. Here, we describe a novel role for PARP1 and PARP2 in regulating Rad52-dependent replication fork repair to maintain cell viability when homologous recombination is dysfunctional, suppress replication-associated DNA damage, and maintain genome stability. Mechanistically, Mre11 and ATM are required for induction of PARP activity in response to replication stress that in turn promotes break-induced replication (BIR) through assembly of Rad52 at stalled/damaged replication forks. Further, by mapping ADP-ribosylation sites induced upon replication stress, we identify that PolD3 is a target for PARP1/PARP2 and that its site-specific ADP-ribosylation is required for BIR activity, replication fork recovery and genome stability. Overall, these data identify a critical role for Mre11-dependent PARP activation and site-specific ADP-ribosylation in regulating BIR to maintain genome integrity during DNA synthesis.

AB - Although Poly(ADP-ribose)-polymerases (PARPs) are key regulators of genome stability, how site-specific ADP-ribosylation regulates DNA repair is unclear. Here, we describe a novel role for PARP1 and PARP2 in regulating Rad52-dependent replication fork repair to maintain cell viability when homologous recombination is dysfunctional, suppress replication-associated DNA damage, and maintain genome stability. Mechanistically, Mre11 and ATM are required for induction of PARP activity in response to replication stress that in turn promotes break-induced replication (BIR) through assembly of Rad52 at stalled/damaged replication forks. Further, by mapping ADP-ribosylation sites induced upon replication stress, we identify that PolD3 is a target for PARP1/PARP2 and that its site-specific ADP-ribosylation is required for BIR activity, replication fork recovery and genome stability. Overall, these data identify a critical role for Mre11-dependent PARP activation and site-specific ADP-ribosylation in regulating BIR to maintain genome integrity during DNA synthesis.

U2 - 10.1038/s41467-023-40071-w

DO - 10.1038/s41467-023-40071-w

M3 - Journal article

C2 - 37463936

AN - SCOPUS:85165400263

VL - 14

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4310

ER -

ID: 363059076