Targeting DNA-Protein Crosslinks via Post-Translational Modifications

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

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Targeting DNA-Protein Crosslinks via Post-Translational Modifications. / Leng, Xueyuan; Duxin, Julien P.

I: Frontiers in Molecular Biosciences, Bind 9, 944775, 2022.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Leng, X & Duxin, JP 2022, 'Targeting DNA-Protein Crosslinks via Post-Translational Modifications', Frontiers in Molecular Biosciences, bind 9, 944775. https://doi.org/10.3389/fmolb.2022.944775

APA

Leng, X., & Duxin, J. P. (2022). Targeting DNA-Protein Crosslinks via Post-Translational Modifications. Frontiers in Molecular Biosciences, 9, [944775]. https://doi.org/10.3389/fmolb.2022.944775

Vancouver

Leng X, Duxin JP. Targeting DNA-Protein Crosslinks via Post-Translational Modifications. Frontiers in Molecular Biosciences. 2022;9. 944775. https://doi.org/10.3389/fmolb.2022.944775

Author

Leng, Xueyuan ; Duxin, Julien P. / Targeting DNA-Protein Crosslinks via Post-Translational Modifications. I: Frontiers in Molecular Biosciences. 2022 ; Bind 9.

Bibtex

@article{029a88f0671f4c0ebc525015ad2cfb3c,
title = "Targeting DNA-Protein Crosslinks via Post-Translational Modifications",
abstract = "Covalent binding of proteins to DNA forms DNA-protein crosslinks (DPCs), which represent cytotoxic DNA lesions that interfere with essential processes such as DNA replication and transcription. Cells possess different enzymatic activities to counteract DPCs. These include enzymes that degrade the adducted proteins, resolve the crosslinks, or incise the DNA to remove the crosslinked proteins. An important question is how DPCs are sensed and targeted for removal via the most suited pathway. Recent advances have shown the inherent role of DNA replication in triggering DPC removal by proteolysis. However, DPCs are also efficiently sensed and removed in the absence of DNA replication. In either scenario, post-translational modifications (PTMs) on DPCs play essential and versatile roles in orchestrating the repair routes. In this review, we summarize the current knowledge of the mechanisms that trigger DPC removal via PTMs, focusing on ubiquitylation, small ubiquitin-related modifier (SUMO) conjugation (SUMOylation), and poly (ADP-ribosyl)ation (PARylation). We also briefly discuss the current knowledge gaps and emerging hypotheses in the field.",
author = "Xueyuan Leng and Duxin, {Julien P.}",
note = "Copyright {\textcopyright} 2022 Leng and Duxin.",
year = "2022",
doi = "10.3389/fmolb.2022.944775",
language = "English",
volume = "9",
journal = "Frontiers in Molecular Biosciences",
issn = "2296-889X",
publisher = "Frontiers Media",

}

RIS

TY - JOUR

T1 - Targeting DNA-Protein Crosslinks via Post-Translational Modifications

AU - Leng, Xueyuan

AU - Duxin, Julien P.

N1 - Copyright © 2022 Leng and Duxin.

PY - 2022

Y1 - 2022

N2 - Covalent binding of proteins to DNA forms DNA-protein crosslinks (DPCs), which represent cytotoxic DNA lesions that interfere with essential processes such as DNA replication and transcription. Cells possess different enzymatic activities to counteract DPCs. These include enzymes that degrade the adducted proteins, resolve the crosslinks, or incise the DNA to remove the crosslinked proteins. An important question is how DPCs are sensed and targeted for removal via the most suited pathway. Recent advances have shown the inherent role of DNA replication in triggering DPC removal by proteolysis. However, DPCs are also efficiently sensed and removed in the absence of DNA replication. In either scenario, post-translational modifications (PTMs) on DPCs play essential and versatile roles in orchestrating the repair routes. In this review, we summarize the current knowledge of the mechanisms that trigger DPC removal via PTMs, focusing on ubiquitylation, small ubiquitin-related modifier (SUMO) conjugation (SUMOylation), and poly (ADP-ribosyl)ation (PARylation). We also briefly discuss the current knowledge gaps and emerging hypotheses in the field.

AB - Covalent binding of proteins to DNA forms DNA-protein crosslinks (DPCs), which represent cytotoxic DNA lesions that interfere with essential processes such as DNA replication and transcription. Cells possess different enzymatic activities to counteract DPCs. These include enzymes that degrade the adducted proteins, resolve the crosslinks, or incise the DNA to remove the crosslinked proteins. An important question is how DPCs are sensed and targeted for removal via the most suited pathway. Recent advances have shown the inherent role of DNA replication in triggering DPC removal by proteolysis. However, DPCs are also efficiently sensed and removed in the absence of DNA replication. In either scenario, post-translational modifications (PTMs) on DPCs play essential and versatile roles in orchestrating the repair routes. In this review, we summarize the current knowledge of the mechanisms that trigger DPC removal via PTMs, focusing on ubiquitylation, small ubiquitin-related modifier (SUMO) conjugation (SUMOylation), and poly (ADP-ribosyl)ation (PARylation). We also briefly discuss the current knowledge gaps and emerging hypotheses in the field.

U2 - 10.3389/fmolb.2022.944775

DO - 10.3389/fmolb.2022.944775

M3 - Review

C2 - 35860355

VL - 9

JO - Frontiers in Molecular Biosciences

JF - Frontiers in Molecular Biosciences

SN - 2296-889X

M1 - 944775

ER -

ID: 314631455