Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links

Research output: Contribution to journalJournal articlepeer-review

Standard

Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. / Räschle, Markus; Smeenk, Godelieve; Hansen, Rebecca K; Temu, Tikira; Oka, Yasuyoshi; Hein, Marco Y; Nagaraj, Nagarjuna; Long, David T; Walter, Johannes C; Hofmann, Kay; Storchova, Zuzana; Cox, Jürgen; Bekker-Jensen, Simon; Mailand, Niels; Mann, Matthias.

In: Science, Vol. 348, No. 6234, 1253671, 2015, p. 539-.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Räschle, M, Smeenk, G, Hansen, RK, Temu, T, Oka, Y, Hein, MY, Nagaraj, N, Long, DT, Walter, JC, Hofmann, K, Storchova, Z, Cox, J, Bekker-Jensen, S, Mailand, N & Mann, M 2015, 'Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links', Science, vol. 348, no. 6234, 1253671, pp. 539-. https://doi.org/10.1126/science.1253671

APA

Räschle, M., Smeenk, G., Hansen, R. K., Temu, T., Oka, Y., Hein, M. Y., Nagaraj, N., Long, D. T., Walter, J. C., Hofmann, K., Storchova, Z., Cox, J., Bekker-Jensen, S., Mailand, N., & Mann, M. (2015). Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Science, 348(6234), 539-. [1253671]. https://doi.org/10.1126/science.1253671

Vancouver

Räschle M, Smeenk G, Hansen RK, Temu T, Oka Y, Hein MY et al. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Science. 2015;348(6234):539-. 1253671. https://doi.org/10.1126/science.1253671

Author

Räschle, Markus ; Smeenk, Godelieve ; Hansen, Rebecca K ; Temu, Tikira ; Oka, Yasuyoshi ; Hein, Marco Y ; Nagaraj, Nagarjuna ; Long, David T ; Walter, Johannes C ; Hofmann, Kay ; Storchova, Zuzana ; Cox, Jürgen ; Bekker-Jensen, Simon ; Mailand, Niels ; Mann, Matthias. / Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. In: Science. 2015 ; Vol. 348, No. 6234. pp. 539-.

Bibtex

@article{b4d7c700b4554589bd257f4b1ead8c90,
title = "Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links",
abstract = "DNA interstrand cross-links (ICLs) block replication fork progression by inhibiting DNA strand separation. Repair of ICLs requires sequential incisions, translesion DNA synthesis, and homologous recombination, but the full set of factors involved in these transactions remains unknown. We devised a technique called chromatin mass spectrometry (CHROMASS) to study protein recruitment dynamics during perturbed DNA replication in Xenopus egg extracts. Using CHROMASS, we systematically monitored protein assembly and disassembly on ICL-containing chromatin. Among numerous prospective DNA repair factors, we identified SLF1 and SLF2, which form a complex with RAD18 and together define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions. Our study provides a global analysis of an entire DNA repair pathway and reveals the mechanism of SMC5/6 relocalization to damaged DNA in vertebrate cells.",
keywords = "Animals, Chromatin, DNA Damage, DNA Repair, DNA Repair Enzymes, DNA Replication, DNA-Binding Proteins, Mass Spectrometry, Proteomics, RNA-Binding Proteins, Xenopus",
author = "Markus R{\"a}schle and Godelieve Smeenk and Hansen, {Rebecca K} and Tikira Temu and Yasuyoshi Oka and Hein, {Marco Y} and Nagarjuna Nagaraj and Long, {David T} and Walter, {Johannes C} and Kay Hofmann and Zuzana Storchova and J{\"u}rgen Cox and Simon Bekker-Jensen and Niels Mailand and Matthias Mann",
note = "Copyright {\textcopyright} 2015, American Association for the Advancement of Science.",
year = "2015",
doi = "10.1126/science.1253671",
language = "English",
volume = "348",
pages = "539--",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6234",

}

RIS

TY - JOUR

T1 - Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links

AU - Räschle, Markus

AU - Smeenk, Godelieve

AU - Hansen, Rebecca K

AU - Temu, Tikira

AU - Oka, Yasuyoshi

AU - Hein, Marco Y

AU - Nagaraj, Nagarjuna

AU - Long, David T

AU - Walter, Johannes C

AU - Hofmann, Kay

AU - Storchova, Zuzana

AU - Cox, Jürgen

AU - Bekker-Jensen, Simon

AU - Mailand, Niels

AU - Mann, Matthias

N1 - Copyright © 2015, American Association for the Advancement of Science.

PY - 2015

Y1 - 2015

N2 - DNA interstrand cross-links (ICLs) block replication fork progression by inhibiting DNA strand separation. Repair of ICLs requires sequential incisions, translesion DNA synthesis, and homologous recombination, but the full set of factors involved in these transactions remains unknown. We devised a technique called chromatin mass spectrometry (CHROMASS) to study protein recruitment dynamics during perturbed DNA replication in Xenopus egg extracts. Using CHROMASS, we systematically monitored protein assembly and disassembly on ICL-containing chromatin. Among numerous prospective DNA repair factors, we identified SLF1 and SLF2, which form a complex with RAD18 and together define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions. Our study provides a global analysis of an entire DNA repair pathway and reveals the mechanism of SMC5/6 relocalization to damaged DNA in vertebrate cells.

AB - DNA interstrand cross-links (ICLs) block replication fork progression by inhibiting DNA strand separation. Repair of ICLs requires sequential incisions, translesion DNA synthesis, and homologous recombination, but the full set of factors involved in these transactions remains unknown. We devised a technique called chromatin mass spectrometry (CHROMASS) to study protein recruitment dynamics during perturbed DNA replication in Xenopus egg extracts. Using CHROMASS, we systematically monitored protein assembly and disassembly on ICL-containing chromatin. Among numerous prospective DNA repair factors, we identified SLF1 and SLF2, which form a complex with RAD18 and together define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions. Our study provides a global analysis of an entire DNA repair pathway and reveals the mechanism of SMC5/6 relocalization to damaged DNA in vertebrate cells.

KW - Animals

KW - Chromatin

KW - DNA Damage

KW - DNA Repair

KW - DNA Repair Enzymes

KW - DNA Replication

KW - DNA-Binding Proteins

KW - Mass Spectrometry

KW - Proteomics

KW - RNA-Binding Proteins

KW - Xenopus

U2 - 10.1126/science.1253671

DO - 10.1126/science.1253671

M3 - Journal article

C2 - 25931565

VL - 348

SP - 539-

JO - Science

JF - Science

SN - 0036-8075

IS - 6234

M1 - 1253671

ER -

ID: 140238644