LEDGF (p75) promotes DNA-end resection and homologous recombination

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

LEDGF (p75) promotes DNA-end resection and homologous recombination. / Daugaard, Mads; Baude, Annika; Fugger, Kasper; Povlsen, Lou Klitgaard; Beck, Halfdan; Sørensen, Claus Storgaard; Petersen, Nikolaj H T; Sorensen, Poul H B; Lukas, Claudia; Bartek, Jiri; Lukas, Jiri; Rohde, Mikkel; Jaattela, Marja.

In: Nature Structural & Molecular Biology, Vol. 19, No. 8, 08.2012, p. 803-810.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Daugaard, M, Baude, A, Fugger, K, Povlsen, LK, Beck, H, Sørensen, CS, Petersen, NHT, Sorensen, PHB, Lukas, C, Bartek, J, Lukas, J, Rohde, M & Jaattela, M 2012, 'LEDGF (p75) promotes DNA-end resection and homologous recombination', Nature Structural & Molecular Biology, vol. 19, no. 8, pp. 803-810. https://doi.org/10.1038/nsmb.2314

APA

Daugaard, M., Baude, A., Fugger, K., Povlsen, L. K., Beck, H., Sørensen, C. S., Petersen, N. H. T., Sorensen, P. H. B., Lukas, C., Bartek, J., Lukas, J., Rohde, M., & Jaattela, M. (2012). LEDGF (p75) promotes DNA-end resection and homologous recombination. Nature Structural & Molecular Biology, 19(8), 803-810. https://doi.org/10.1038/nsmb.2314

Vancouver

Daugaard M, Baude A, Fugger K, Povlsen LK, Beck H, Sørensen CS et al. LEDGF (p75) promotes DNA-end resection and homologous recombination. Nature Structural & Molecular Biology. 2012 Aug;19(8):803-810. https://doi.org/10.1038/nsmb.2314

Author

Daugaard, Mads ; Baude, Annika ; Fugger, Kasper ; Povlsen, Lou Klitgaard ; Beck, Halfdan ; Sørensen, Claus Storgaard ; Petersen, Nikolaj H T ; Sorensen, Poul H B ; Lukas, Claudia ; Bartek, Jiri ; Lukas, Jiri ; Rohde, Mikkel ; Jaattela, Marja. / LEDGF (p75) promotes DNA-end resection and homologous recombination. In: Nature Structural & Molecular Biology. 2012 ; Vol. 19, No. 8. pp. 803-810.

Bibtex

@article{0fedd54f9b36490cb62a634e1b98e28c,
title = "LEDGF (p75) promotes DNA-end resection and homologous recombination",
abstract = "Lens epithelium-derived growth factor p75 splice variant (LEDGF) is a chromatin-binding protein known for its antiapoptotic activity and ability to direct human immunodeficiency virus into active transcription units. Here we show that LEDGF promotes the repair of DNA double-strand breaks (DSBs) by the homologous recombination repair pathway. Depletion of LEDGF impairs the recruitment of C-terminal binding protein interacting protein (CtIP) to DNA DSBs and the subsequent CtIP-dependent DNA-end resection. LEDGF is constitutively associated with chromatin through its Pro-Trp-Trp-Pro (PWWP) domain that binds preferentially to epigenetic methyl-lysine histone markers characteristic of active transcription units. LEDGF binds CtIP in a DNA damage-dependent manner, thereby enhancing its tethering to the active chromatin and facilitating its access to DNA DSBs. These data highlight the role of PWWP-domain proteins in DNA repair and provide a molecular explanation for the antiapoptotic and cancer cell survival-activities of LEDGF.",
author = "Mads Daugaard and Annika Baude and Kasper Fugger and Povlsen, {Lou Klitgaard} and Halfdan Beck and S{\o}rensen, {Claus Storgaard} and Petersen, {Nikolaj H T} and Sorensen, {Poul H B} and Claudia Lukas and Jiri Bartek and Jiri Lukas and Mikkel Rohde and Marja Jaattela",
year = "2012",
month = aug,
doi = "10.1038/nsmb.2314",
language = "English",
volume = "19",
pages = "803--810",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "8",

}

RIS

TY - JOUR

T1 - LEDGF (p75) promotes DNA-end resection and homologous recombination

AU - Daugaard, Mads

AU - Baude, Annika

AU - Fugger, Kasper

AU - Povlsen, Lou Klitgaard

AU - Beck, Halfdan

AU - Sørensen, Claus Storgaard

AU - Petersen, Nikolaj H T

AU - Sorensen, Poul H B

AU - Lukas, Claudia

AU - Bartek, Jiri

AU - Lukas, Jiri

AU - Rohde, Mikkel

AU - Jaattela, Marja

PY - 2012/8

Y1 - 2012/8

N2 - Lens epithelium-derived growth factor p75 splice variant (LEDGF) is a chromatin-binding protein known for its antiapoptotic activity and ability to direct human immunodeficiency virus into active transcription units. Here we show that LEDGF promotes the repair of DNA double-strand breaks (DSBs) by the homologous recombination repair pathway. Depletion of LEDGF impairs the recruitment of C-terminal binding protein interacting protein (CtIP) to DNA DSBs and the subsequent CtIP-dependent DNA-end resection. LEDGF is constitutively associated with chromatin through its Pro-Trp-Trp-Pro (PWWP) domain that binds preferentially to epigenetic methyl-lysine histone markers characteristic of active transcription units. LEDGF binds CtIP in a DNA damage-dependent manner, thereby enhancing its tethering to the active chromatin and facilitating its access to DNA DSBs. These data highlight the role of PWWP-domain proteins in DNA repair and provide a molecular explanation for the antiapoptotic and cancer cell survival-activities of LEDGF.

AB - Lens epithelium-derived growth factor p75 splice variant (LEDGF) is a chromatin-binding protein known for its antiapoptotic activity and ability to direct human immunodeficiency virus into active transcription units. Here we show that LEDGF promotes the repair of DNA double-strand breaks (DSBs) by the homologous recombination repair pathway. Depletion of LEDGF impairs the recruitment of C-terminal binding protein interacting protein (CtIP) to DNA DSBs and the subsequent CtIP-dependent DNA-end resection. LEDGF is constitutively associated with chromatin through its Pro-Trp-Trp-Pro (PWWP) domain that binds preferentially to epigenetic methyl-lysine histone markers characteristic of active transcription units. LEDGF binds CtIP in a DNA damage-dependent manner, thereby enhancing its tethering to the active chromatin and facilitating its access to DNA DSBs. These data highlight the role of PWWP-domain proteins in DNA repair and provide a molecular explanation for the antiapoptotic and cancer cell survival-activities of LEDGF.

U2 - 10.1038/nsmb.2314

DO - 10.1038/nsmb.2314

M3 - Journal article

C2 - 22773103

VL - 19

SP - 803

EP - 810

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 8

ER -

ID: 38488448