Identification of the MMS22L-TONSL complex that promotes homologous recombination

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

Standard

Identification of the MMS22L-TONSL complex that promotes homologous recombination. / Duro, Eris; Lundin, Cecilia; Ask, Katrine; Sanchez-Pulido, Luis; MacArtney, Thomas J; Toth, Rachel; Ponting, Chris P; Groth, Anja; Helleday, Thomas; Rouse, John.

In: Molecular Cell, Vol. 40, No. 4, 24.11.2010, p. 632-44.

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

Harvard

Duro, E, Lundin, C, Ask, K, Sanchez-Pulido, L, MacArtney, TJ, Toth, R, Ponting, CP, Groth, A, Helleday, T & Rouse, J 2010, 'Identification of the MMS22L-TONSL complex that promotes homologous recombination', Molecular Cell, vol. 40, no. 4, pp. 632-44. https://doi.org/10.1016/j.molcel.2010.10.023

APA

Duro, E., Lundin, C., Ask, K., Sanchez-Pulido, L., MacArtney, T. J., Toth, R., Ponting, C. P., Groth, A., Helleday, T., & Rouse, J. (2010). Identification of the MMS22L-TONSL complex that promotes homologous recombination. Molecular Cell, 40(4), 632-44. https://doi.org/10.1016/j.molcel.2010.10.023

Vancouver

Duro E, Lundin C, Ask K, Sanchez-Pulido L, MacArtney TJ, Toth R et al. Identification of the MMS22L-TONSL complex that promotes homologous recombination. Molecular Cell. 2010 Nov 24;40(4):632-44. https://doi.org/10.1016/j.molcel.2010.10.023

Author

Duro, Eris ; Lundin, Cecilia ; Ask, Katrine ; Sanchez-Pulido, Luis ; MacArtney, Thomas J ; Toth, Rachel ; Ponting, Chris P ; Groth, Anja ; Helleday, Thomas ; Rouse, John. / Identification of the MMS22L-TONSL complex that promotes homologous recombination. In: Molecular Cell. 2010 ; Vol. 40, No. 4. pp. 632-44.

Bibtex

@article{73e13ee74fb048db98a9f209d58fe885,
title = "Identification of the MMS22L-TONSL complex that promotes homologous recombination",
abstract = "Budding yeast Mms22 is required for homologous recombination (HR)-mediated repair of stalled or broken DNA replication forks. Here we identify a human Mms22-like protein (MMS22L) and an MMS22L-interacting protein, NF¿BIL2/TONSL. Depletion of MMS22L or TONSL from human cells causes a high level of double-strand breaks (DSBs) during DNA replication. Both proteins accumulate at stressed replication forks, and depletion of MMS22L or TONSL from cells causes hypersensitivity to agents that cause S phase-associated DSBs, such as topoisomerase (TOP) inhibitors. In this light, MMS22L and TONSL are required for the HR-mediated repair of replication fork-associated DSBs. In cells depleted of either protein, DSBs induced by the TOP1 inhibitor camptothecin are resected normally, but the loading of the RAD51 recombinase is defective. Therefore, MMS22L and TONSL are required for the maintenance of genome stability when unscheduled DSBs occur in the vicinity of DNA replication forks.",
keywords = "Amino Acid Sequence, Cell Cycle Proteins, Cell Line, Cell Survival, Computational Biology, DNA Breaks, Double-Stranded, DNA-Binding Proteins, DNA-Directed DNA Polymerase, Drug Resistance, Humans, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Multiprotein Complexes, NF-kappa B, Nuclear Proteins, Protein Binding, Rad51 Recombinase, Recombination, Genetic, S Phase",
author = "Eris Duro and Cecilia Lundin and Katrine Ask and Luis Sanchez-Pulido and MacArtney, {Thomas J} and Rachel Toth and Ponting, {Chris P} and Anja Groth and Thomas Helleday and John Rouse",
note = "Copyright {\textcopyright} 2010 Elsevier Inc. All rights reserved.",
year = "2010",
month = nov,
day = "24",
doi = "10.1016/j.molcel.2010.10.023",
language = "English",
volume = "40",
pages = "632--44",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - Identification of the MMS22L-TONSL complex that promotes homologous recombination

AU - Duro, Eris

AU - Lundin, Cecilia

AU - Ask, Katrine

AU - Sanchez-Pulido, Luis

AU - MacArtney, Thomas J

AU - Toth, Rachel

AU - Ponting, Chris P

AU - Groth, Anja

AU - Helleday, Thomas

AU - Rouse, John

N1 - Copyright © 2010 Elsevier Inc. All rights reserved.

PY - 2010/11/24

Y1 - 2010/11/24

N2 - Budding yeast Mms22 is required for homologous recombination (HR)-mediated repair of stalled or broken DNA replication forks. Here we identify a human Mms22-like protein (MMS22L) and an MMS22L-interacting protein, NF¿BIL2/TONSL. Depletion of MMS22L or TONSL from human cells causes a high level of double-strand breaks (DSBs) during DNA replication. Both proteins accumulate at stressed replication forks, and depletion of MMS22L or TONSL from cells causes hypersensitivity to agents that cause S phase-associated DSBs, such as topoisomerase (TOP) inhibitors. In this light, MMS22L and TONSL are required for the HR-mediated repair of replication fork-associated DSBs. In cells depleted of either protein, DSBs induced by the TOP1 inhibitor camptothecin are resected normally, but the loading of the RAD51 recombinase is defective. Therefore, MMS22L and TONSL are required for the maintenance of genome stability when unscheduled DSBs occur in the vicinity of DNA replication forks.

AB - Budding yeast Mms22 is required for homologous recombination (HR)-mediated repair of stalled or broken DNA replication forks. Here we identify a human Mms22-like protein (MMS22L) and an MMS22L-interacting protein, NF¿BIL2/TONSL. Depletion of MMS22L or TONSL from human cells causes a high level of double-strand breaks (DSBs) during DNA replication. Both proteins accumulate at stressed replication forks, and depletion of MMS22L or TONSL from cells causes hypersensitivity to agents that cause S phase-associated DSBs, such as topoisomerase (TOP) inhibitors. In this light, MMS22L and TONSL are required for the HR-mediated repair of replication fork-associated DSBs. In cells depleted of either protein, DSBs induced by the TOP1 inhibitor camptothecin are resected normally, but the loading of the RAD51 recombinase is defective. Therefore, MMS22L and TONSL are required for the maintenance of genome stability when unscheduled DSBs occur in the vicinity of DNA replication forks.

KW - Amino Acid Sequence

KW - Cell Cycle Proteins

KW - Cell Line

KW - Cell Survival

KW - Computational Biology

KW - DNA Breaks, Double-Stranded

KW - DNA-Binding Proteins

KW - DNA-Directed DNA Polymerase

KW - Drug Resistance

KW - Humans

KW - Models, Biological

KW - Molecular Sequence Data

KW - Multienzyme Complexes

KW - Multiprotein Complexes

KW - NF-kappa B

KW - Nuclear Proteins

KW - Protein Binding

KW - Rad51 Recombinase

KW - Recombination, Genetic

KW - S Phase

U2 - 10.1016/j.molcel.2010.10.023

DO - 10.1016/j.molcel.2010.10.023

M3 - Journal article

C2 - 21055984

VL - 40

SP - 632

EP - 644

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -

ID: 32309672