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RanBP2-mediated SUMOylation promotes human DNA polymerase lambda nuclear localization and DNA repair

M. Moreno-Oñate, A.M. Herrero-Ruiz, M. García-Dominguez, F. Cortés-Ledesma, J.F. Ruiz
doi: https://doi.org/10.1101/2020.02.14.949644
M. Moreno-Oñate
1Departamento Bioquímica Vegetal y Biología Molecular, Universidad de Sevilla, 41012 Sevilla, Spain
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A.M. Herrero-Ruiz
2Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER) Universidad de Sevilla/CSIC/Universidad Pablo Olavide/Junta de Andalucía, 41092 Sevilla, Spain
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M. García-Dominguez
2Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER) Universidad de Sevilla/CSIC/Universidad Pablo Olavide/Junta de Andalucía, 41092 Sevilla, Spain
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F. Cortés-Ledesma
2Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER) Universidad de Sevilla/CSIC/Universidad Pablo Olavide/Junta de Andalucía, 41092 Sevilla, Spain
3Topology and DNA breaks group, Spanish National Cancer Research Centre (CNIO), 28029 Madrid, Spain
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  • For correspondence: jfruiz@us.es fcortes@cnio.es
J.F. Ruiz
1Departamento Bioquímica Vegetal y Biología Molecular, Universidad de Sevilla, 41012 Sevilla, Spain
2Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER) Universidad de Sevilla/CSIC/Universidad Pablo Olavide/Junta de Andalucía, 41092 Sevilla, Spain
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  • For correspondence: jfruiz@us.es fcortes@cnio.es
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Abstract

Cellular DNA is under constant attack by a wide variety of agents, both endogenous and exogenous. To counteract DNA damage, human cells have a large collection of DNA repair factors. Among them, DNA polymerase lambda (Polλ) stands out for its versatility, as it participates in different DNA repair and damage tolerance pathways in which gap-filling DNA synthesis is required. In this work we show that human Polλ is conjugated with Small Ubiquitin-like MOdifier (SUMO) proteins both in vitro and in vivo, with Lys27 being the main target of this covalent modification. Polλ SUMOylation takes place in the nuclear pore complex and is mediated by the E3 ligase RanBP2. This post-translational modification promotes Polλ entry into the nucleus, which is required for its recruitment to DNA lesions and stimulated by DNA damage induction. Our work represents an advance in the knowledge of molecular pathways that regulate cellular localization of human Polλ, which are essential to be able to perform its functions during repair of nuclear DNA, and that might constitute an important point for the modulation of its activity in human cells.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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Posted February 15, 2020.
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RanBP2-mediated SUMOylation promotes human DNA polymerase lambda nuclear localization and DNA repair
M. Moreno-Oñate, A.M. Herrero-Ruiz, M. García-Dominguez, F. Cortés-Ledesma, J.F. Ruiz
bioRxiv 2020.02.14.949644; doi: https://doi.org/10.1101/2020.02.14.949644
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RanBP2-mediated SUMOylation promotes human DNA polymerase lambda nuclear localization and DNA repair
M. Moreno-Oñate, A.M. Herrero-Ruiz, M. García-Dominguez, F. Cortés-Ledesma, J.F. Ruiz
bioRxiv 2020.02.14.949644; doi: https://doi.org/10.1101/2020.02.14.949644

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