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Article: Timeless Interacts with PARP-1 to Promote Homologous Recombination Repair

TitleTimeless Interacts with PARP-1 to Promote Homologous Recombination Repair
Authors
Issue Date2015
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel
Citation
Molecular Cell, 2015, v. 60 n. 1, p. 163-176 How to Cite?
AbstractHuman Timeless helps stabilize replication forks during normal DNA replication and plays a critical role in activation of the S phase checkpoint and proper establishment of sister chromatid cohesion. However, it remains elusive whether Timeless is involved in the repair of damaged DNA. Here, we identify that Timeless physically interacts with PARP-1 independent of poly(ADP-ribosyl)ation. We present high-resolution crystal structures of Timeless PAB (PARP-1-binding domain) in free form and in complex with PARP-1 catalytic domain. Interestingly, Timeless PAB domain specifically recognizes PARP-1, but not PARP-2 or PARP-3. Timeless-PARP-1 interaction does not interfere with PARP-1 enzymatic activity. We demonstrate that rapid and transient accumulation of Timeless at laser-induced DNA damage sites requires PARP-1, but not poly(ADP-ribosyl)ation and that Timeless is co-trapped with PARP-1 at DNA lesions upon PARP inhibition. Furthermore, we show that Timeless and PARP-1 interaction is required for efficient homologous recombination repair.
Persistent Identifierhttp://hdl.handle.net/10722/216598
ISSN
2023 Impact Factor: 14.5
2023 SCImago Journal Rankings: 9.332
ISI Accession Number ID
Errata

 

DC FieldValueLanguage
dc.contributor.authorXie, S-
dc.contributor.authorMortusewicz, O-
dc.contributor.authorMa, HT-
dc.contributor.authorHerr, P-
dc.contributor.authorPoon, RYC-
dc.contributor.authorHelleday, T-
dc.contributor.authorQian, C-
dc.date.accessioned2015-09-18T05:33:21Z-
dc.date.available2015-09-18T05:33:21Z-
dc.date.issued2015-
dc.identifier.citationMolecular Cell, 2015, v. 60 n. 1, p. 163-176-
dc.identifier.issn1097-2765-
dc.identifier.urihttp://hdl.handle.net/10722/216598-
dc.description.abstractHuman Timeless helps stabilize replication forks during normal DNA replication and plays a critical role in activation of the S phase checkpoint and proper establishment of sister chromatid cohesion. However, it remains elusive whether Timeless is involved in the repair of damaged DNA. Here, we identify that Timeless physically interacts with PARP-1 independent of poly(ADP-ribosyl)ation. We present high-resolution crystal structures of Timeless PAB (PARP-1-binding domain) in free form and in complex with PARP-1 catalytic domain. Interestingly, Timeless PAB domain specifically recognizes PARP-1, but not PARP-2 or PARP-3. Timeless-PARP-1 interaction does not interfere with PARP-1 enzymatic activity. We demonstrate that rapid and transient accumulation of Timeless at laser-induced DNA damage sites requires PARP-1, but not poly(ADP-ribosyl)ation and that Timeless is co-trapped with PARP-1 at DNA lesions upon PARP inhibition. Furthermore, we show that Timeless and PARP-1 interaction is required for efficient homologous recombination repair.-
dc.languageeng-
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel-
dc.relation.ispartofMolecular Cell-
dc.titleTimeless Interacts with PARP-1 to Promote Homologous Recombination Repair-
dc.typeArticle-
dc.identifier.emailXie, S: xiesi@hku.hk-
dc.identifier.emailMa, HT: kenhtma@hku.hk-
dc.identifier.emailQian, C: cmqian@hku.hk-
dc.identifier.authorityMa, HT=rp02894-
dc.identifier.authorityQian, C=rp01371-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.molcel.2015.07.031-
dc.identifier.pmid26344098-
dc.identifier.scopuseid_2-s2.0-84952873902-
dc.identifier.hkuros253633-
dc.identifier.volume60-
dc.identifier.issue1-
dc.identifier.spage163-
dc.identifier.epage176-
dc.identifier.isiWOS:000366585100015-
dc.publisher.placeUnited States-
dc.relation.erratumdoi:10.1016/j.molcel.2015.12.019-
dc.relation.erratumeid:eid_2-s2.0-84953383188-
dc.identifier.f1000725773074-

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