elib
DLR-Header
DLR-Logo -> http://www.dlr.de
DLR Portal Home | Imprint | Privacy Policy | Contact | Deutsch
Fontsize: [-] Text [+]

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

de Ory, Ana and Nagler, Katja and Carrasco, Begoña and Raguse, Marina and Zafra, Olga and Moeller, Ralf and de Vega, Miguel (2016) Identification of a conserved 5′-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair. Nucleic Acids Research, 44 (4), pp. 1833-1844. Oxford University Press. DOI: 10.1093/nar/gkw054 ISSN 0305-1048

[img] PDF
2MB

Official URL: http://dx.doi.org/10.1093/nar/gkw054

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.

Item URL in elib:https://elib.dlr.de/104006/
Document Type:Article
Title:Identification of a conserved 5′-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair
Authors:
AuthorsInstitution or Email of AuthorsAuthors ORCID iD
de Ory, AnaCentro de Biologia Molecular ‘Severo Ochoa’ (Consejo Superior de Investigaciones Cientificas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, SpainUNSPECIFIED
Nagler, KatjaRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, GermanyUNSPECIFIED
Carrasco, BegoñaCentro Nacional de Biotecnologia (Consejo Superior de Investigaciones Cientificas), Darwin 3, 28049 Madrid, SpainUNSPECIFIED
Raguse, MarinaRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, GermanyUNSPECIFIED
Zafra, OlgaCentro de Biologia Molecular ‘Severo Ochoa’ (Consejo Superior de Investigaciones Cientificas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, SpainUNSPECIFIED
Moeller, RalfRadiation Biology Department, German Aerospace Center (DLR), Institute of Aerospace Medicine, Linder Hoehe, D-51147 Cologne, GermanyUNSPECIFIED
de Vega, MiguelCentro de Biologia Molecular ‘Severo Ochoa’ (Consejo Superior de Investigaciones Cientificas-Universidad Autónoma de Madrid), Nicolás Cabrera 1, 28049 Madrid, SpainUNSPECIFIED
Date:2016
Journal or Publication Title:Nucleic Acids Research
Refereed publication:Yes
Open Access:Yes
Gold Open Access:Yes
In SCOPUS:Yes
In ISI Web of Science:Yes
Volume:44
DOI :10.1093/nar/gkw054
Page Range:pp. 1833-1844
Publisher:Oxford University Press
ISSN:0305-1048
Status:Published
Keywords:Bacillus subtilis, DNA repair, DNA Ligase D (BsuLigD), 5′-dRP lyase activity
HGF - Research field:Aeronautics, Space and Transport
HGF - Program:Space
HGF - Program Themes:Research under Space Conditions
DLR - Research area:Raumfahrt
DLR - Program:R FR - Forschung unter Weltraumbedingungen
DLR - Research theme (Project):R - Vorhaben Strahlenbiologie
Location: Köln-Porz
Institutes and Institutions:Institute of Aerospace Medicine > Radiation Biology
Deposited By: Kopp, Kerstin
Deposited On:19 Apr 2016 09:29
Last Modified:19 Apr 2016 09:29

Repository Staff Only: item control page

Browse
Search
Help & Contact
Information
electronic library is running on EPrints 3.3.12
Copyright © 2008-2017 German Aerospace Center (DLR). All rights reserved.