Repair of a DNA-protein crosslink by replication-coupled proteolysis

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Repair of a DNA-protein crosslink by replication-coupled proteolysis. / Duxin, Julien P; Dewar, James M; Yardimci, Hasan; Walter, Johannes C.

In: Cell, Vol. 159, No. 2, 09.10.2014, p. 346-57.

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

Harvard

Duxin, JP, Dewar, JM, Yardimci, H & Walter, JC 2014, 'Repair of a DNA-protein crosslink by replication-coupled proteolysis', Cell, vol. 159, no. 2, pp. 346-57. https://doi.org/10.1016/j.cell.2014.09.024

APA

Duxin, J. P., Dewar, J. M., Yardimci, H., & Walter, J. C. (2014). Repair of a DNA-protein crosslink by replication-coupled proteolysis. Cell, 159(2), 346-57. https://doi.org/10.1016/j.cell.2014.09.024

Vancouver

Duxin JP, Dewar JM, Yardimci H, Walter JC. Repair of a DNA-protein crosslink by replication-coupled proteolysis. Cell. 2014 Oct 9;159(2):346-57. https://doi.org/10.1016/j.cell.2014.09.024

Author

Duxin, Julien P ; Dewar, James M ; Yardimci, Hasan ; Walter, Johannes C. / Repair of a DNA-protein crosslink by replication-coupled proteolysis. In: Cell. 2014 ; Vol. 159, No. 2. pp. 346-57.

Bibtex

@article{d02a12687a8c4dd8b21e1c4d0ec45923,
title = "Repair of a DNA-protein crosslink by replication-coupled proteolysis",
abstract = "DNA-protein crosslinks (DPCs) are caused by environmental, endogenous, and chemotherapeutic agents and pose a severe threat to genome stability. We use Xenopus egg extracts to recapitulate DPC repair in vitro and show that this process is coupled to DNA replication. A DPC on the leading strand template arrests the replisome by stalling the CMG helicase. The DPC is then degraded on DNA, yielding a peptide-DNA adduct that is bypassed by CMG. The leading strand subsequently resumes synthesis, stalls again at the adduct, and then progresses past the adduct using DNA polymerase ζ. A DPC on the lagging strand template only transiently stalls the replisome, but it too is degraded, allowing Okazaki fragment bypass. Our experiments describe a versatile, proteolysis-based mechanism of S phase DPC repair that avoids replication fork collapse.",
keywords = "Animals, Cell Extracts, DNA Adducts, DNA Repair, DNA Replication, DNA-Directed DNA Polymerase, Genomic Instability, Ovum, Xenopus, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.",
author = "Duxin, {Julien P} and Dewar, {James M} and Hasan Yardimci and Walter, {Johannes C}",
note = "Copyright {\textcopyright} 2014 Elsevier Inc. All rights reserved.",
year = "2014",
month = oct,
day = "9",
doi = "10.1016/j.cell.2014.09.024",
language = "English",
volume = "159",
pages = "346--57",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - Repair of a DNA-protein crosslink by replication-coupled proteolysis

AU - Duxin, Julien P

AU - Dewar, James M

AU - Yardimci, Hasan

AU - Walter, Johannes C

N1 - Copyright © 2014 Elsevier Inc. All rights reserved.

PY - 2014/10/9

Y1 - 2014/10/9

N2 - DNA-protein crosslinks (DPCs) are caused by environmental, endogenous, and chemotherapeutic agents and pose a severe threat to genome stability. We use Xenopus egg extracts to recapitulate DPC repair in vitro and show that this process is coupled to DNA replication. A DPC on the leading strand template arrests the replisome by stalling the CMG helicase. The DPC is then degraded on DNA, yielding a peptide-DNA adduct that is bypassed by CMG. The leading strand subsequently resumes synthesis, stalls again at the adduct, and then progresses past the adduct using DNA polymerase ζ. A DPC on the lagging strand template only transiently stalls the replisome, but it too is degraded, allowing Okazaki fragment bypass. Our experiments describe a versatile, proteolysis-based mechanism of S phase DPC repair that avoids replication fork collapse.

AB - DNA-protein crosslinks (DPCs) are caused by environmental, endogenous, and chemotherapeutic agents and pose a severe threat to genome stability. We use Xenopus egg extracts to recapitulate DPC repair in vitro and show that this process is coupled to DNA replication. A DPC on the leading strand template arrests the replisome by stalling the CMG helicase. The DPC is then degraded on DNA, yielding a peptide-DNA adduct that is bypassed by CMG. The leading strand subsequently resumes synthesis, stalls again at the adduct, and then progresses past the adduct using DNA polymerase ζ. A DPC on the lagging strand template only transiently stalls the replisome, but it too is degraded, allowing Okazaki fragment bypass. Our experiments describe a versatile, proteolysis-based mechanism of S phase DPC repair that avoids replication fork collapse.

KW - Animals

KW - Cell Extracts

KW - DNA Adducts

KW - DNA Repair

KW - DNA Replication

KW - DNA-Directed DNA Polymerase

KW - Genomic Instability

KW - Ovum

KW - Xenopus

KW - Journal Article

KW - Research Support, N.I.H., Extramural

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

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

U2 - 10.1016/j.cell.2014.09.024

DO - 10.1016/j.cell.2014.09.024

M3 - Journal article

C2 - 25303529

VL - 159

SP - 346

EP - 357

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -

ID: 176967569