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http://hdl.handle.net/10261/151612
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Ory, Ana de | - |
dc.contributor.author | Nagler, Katja | - |
dc.contributor.author | Carrasco, Begoña | - |
dc.contributor.author | Raguse, Marina | - |
dc.contributor.author | Zafra, Olga | - |
dc.contributor.author | Moeller, Ralf | - |
dc.contributor.author | Vega, Miguel de | - |
dc.date.accessioned | 2017-06-19T08:29:24Z | - |
dc.date.available | 2017-06-19T08:29:24Z | - |
dc.date.issued | 2016-01-20 | - |
dc.identifier | doi: 10.1093/nar/gkw054 | - |
dc.identifier | issn: 1362-4962 | - |
dc.identifier.citation | Nucleic Acids Research 44: 1833- 1844 (2016) | - |
dc.identifier.uri | http://hdl.handle.net/10261/151612 | - |
dc.description.abstract | Bacillus subtilis is one of the bacterial members provided with a nonhomologous end joining (NHEJ) system constituted by the DNA-binding Ku homodimer that recruits the ATP-dependent DNA Ligase D (BsuLigD) to the double-stranded DNA breaks (DSBs) ends. BsuLigD has inherent polymerization and ligase activities that allow it to fill the short gaps that can arise after realignment of the broken ends and to seal the resulting nicks, contributing to genome stability during the stationary phase and germination of spores. Here we show that BsuLigD also has an intrinsic 5'-2-deoxyribose-5-phosphate (dRP) lyase activity located at the N-terminal ligase domain that in coordination with the polymerization and ligase activities allows efficient repairing of 2'-deoxyuridine-containing DNA in an in vitro reconstituted Base Excision Repair (BER) reaction. The requirement of a polymerization, a dRP removal and a final sealing step in BER, together with the joint participation of BsuLigD with the spore specific AP endonuclease in conferring spore resistance to ultrahigh vacuum desiccation suggest that BsuLigD could actively participate in this pathway. We demonstrate the presence of the dRP lyase activity also in the homolog protein from the distantly related bacterium Pseudomonas aeruginosa, allowing us to expand our results to other bacterial LigDs. | - |
dc.description.sponsorship | Spanish Ministry of Economy and Competitiveness [BFU2014-53791-P to M.V.]; German Aerospace Center [DLR-FuE-Projekt ISS-Nutzung in der Biodiagnostik, Programm RF-FuW, Teilprogramm 475 to R.M.]; German Research Foundation [DFG Paketantrag (PlasmaDecon PAK 728) (MO 2023/2-1) to R.M.]; Fundación Ramón Areces (Institutional Grant to the Centro de Biología Molecular ‘Severo Ochoa’). | - |
dc.publisher | Oxford University Press | - |
dc.relation.isversionof | Publisher's version | - |
dc.rights | openAccess | - |
dc.title | Identification of a conserved 5′-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1093/nar/gkw054 | - |
dc.date.updated | 2017-06-19T08:29:24Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.rights.license | https://creativecommons.org/licenses/by/4.0/ | - |
dc.contributor.funder | German Research Foundation | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.contributor.funder | German Centre for Air and Space Travel | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100001659 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100002946 | es_ES |
dc.identifier.pmid | 26826709 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | open | - |
item.fulltext | With Fulltext | - |
item.openairetype | artículo | - |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
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DeVegaM_IdentficationOfAConserved5´-dRPLyase.pdf | 2,35 MB | Adobe PDF | Visualizar/Abrir |
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