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  Replication-Coupled DNA-Protein Crosslink Repair by SPRTN and the Proteasome in Xenopus Egg Extracts.

Larsen, N. B., Gao, A. O., Sparks, J. L., Gallina, I., Wu, R. A., Mann, M., et al. (2019). Replication-Coupled DNA-Protein Crosslink Repair by SPRTN and the Proteasome in Xenopus Egg Extracts. Molecular Cell, 73(3), 574-588.e7. doi:10.1016/j.molcel.2018.11.024.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-CD53-A Version Permalink: http://hdl.handle.net/21.11116/0000-0004-0338-A
Genre: Journal Article

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 Creators:
Larsen, Nicolai B1, Author
Gao, Alan O1, Author
Sparks, Justin L1, Author
Gallina, Irene1, Author
Wu, R Alex1, Author
Mann, Matthias2, Author              
Raschle, Markus1, Author
Walter, Johannes C1, Author
Duxin, Julien P1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: DNA repair; DNA replication; DNA-portein crosslink (DPC); Proteasome; SPRTN; TRAIP; Ubiquitin; translesion synthesis (TLS)
 Abstract: DNA-protein crosslinks (DPCs) are bulky lesions thatinterfere with DNA metabolism and therefore threaten genomic integrity. Recent studies implicate the metalloprotease SPRTN in S phase removal of DPCs, but how SPRTN is targeted to DPCs during DNA replication is unknown. Using Xenopus egg extracts that recapitulate replication-coupled DPC proteolysis, we show that DPCs can be degraded by SPRTN or the proteasome, which act as independent DPC proteases. Proteasome recruitment requires DPC polyubiquitylation, which is partially dependent on the ubiquitin ligase activity of TRAIP. In contrast, SPRTN-mediated DPC degradation does not require DPC polyubiquitylation but instead depends on nascent strand extension to within a few nucleotides of the lesion, implying that polymerase stalling at the DPC activates SPRTN on both leading and lagging strand templates. Our results demonstrate that SPRTN and proteasome activities are coupled to DNA replication by distinct mechanisms that promote replication across immovable protein barriers. Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.

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Language(s): eng - English
 Dates: 2018-12-272019
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: Data and Software Availability
Perseus is provided by the group of Jürgen Cox at the MPI of Biochemistry and can be freely downloaded at: http://www.coxdocs.org.
 Rev. Method: -
 Identifiers: ISI: 30595436
DOI: 10.1016/j.molcel.2018.11.024
 Degree: -

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Project name : -
Grant ID : 715975
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 73 (3) Sequence Number: - Start / End Page: 574 - 588.e7 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929