English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/151612
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Identification of a conserved 5′-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair

AuthorsOry, Ana de ; Nagler, Katja; Carrasco, Begoña; Raguse, Marina; Zafra, Olga ; Moeller, Ralf; Vega, Miguel de
Issue Date20-Jan-2016
PublisherOxford University Press
CitationNucleic Acids Research 44: 1833- 1844 (2016)
AbstractBacillus 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.
URIhttp://hdl.handle.net/10261/151612
DOI10.1093/nar/gkw054
Identifiersdoi: 10.1093/nar/gkw054
issn: 1362-4962
Appears in Collections:(CBM) Artículos
Files in This Item:
File Description SizeFormat 
DeVegaM_IdentficationOfAConserved5´-dRPLyase.pdf2,35 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.