DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria

Plocinski, Przemyslaw, Brissett, Nigel C, Bianchi, Julie, Brzostek, Anna, Korycka-Machała, Małgorzata, Dziembowski, Andrzej, Dziadek, Jaroslaw and Doherty, Aidan J (2017) DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria. Nature Communications, 1251 (2017). ISSN 2041-1723

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Prokaryotic Ligase D is a conserved DNA repair apparatus processing DNA double-strand breaks in stationary phase. An orthologous Ligase C (LigC) complex also co-exists in many bacterial species but its function is unknown. Here, we show that the LigC complex interacts with core BER enzymes in vivo and demonstrate that together these factors constitute an excision repair apparatus capable of repairing damaged bases and abasic sites. The polymerase component, which contains a conserved C-terminal structural loop, preferentially binds to and fills-in short gapped DNA intermediates with RNA and LigC ligates the resulting nicks to complete repair. Components of the LigC complex, like LigD, are expressed upon entry into stationary phase and cells lacking either of these pathways exhibit increased sensitivity to oxidising genotoxins. Together, these findings establish that the LigC complex is directly involved in an excision repair pathway(s) that repairs DNA damage with ribonucleotides during stationary phase.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Research Centres and Groups: Genome Damage and Stability Centre
Depositing User: Aidan Doherty
Date Deposited: 22 Sep 2017 11:37
Last Modified: 28 Nov 2017 10:21
URI: http://srodev.sussex.ac.uk/id/eprint/70317

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Project NameSussex Project NumberFunderFunder Ref
Cell cycle regulation of the NHEJ DNA double-strand break repair pathway in eukaryotesG1554BBSRC-BIOTECHNOLOGY & BIOLOGICAL SCIENCES RESEARCH COUNCILBB/M004236/1
Molecular basis for repairing DNA double-strand breaks by non homologous end-joiningG0887BBSRC-BIOTECHNOLOGY & BIOLOGICAL SCIENCES RESEARCH COUNCILBB/J018643/1
Understanding the molecular dynamics of NHEJ-mediated synapsisUnsetBBSRCBB/F013795/1