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

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 an...

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Autores principales: Płociński, Przemysław, Brissett, Nigel C., Bianchi, Julie, Brzostek, Anna, Korycka-Machała, Małgorzata, Dziembowski, Andrzej, Dziadek, Jarosław, Doherty, Aidan J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5663958/
https://www.ncbi.nlm.nih.gov/pubmed/29089537
http://dx.doi.org/10.1038/s41467-017-01365-y
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author Płociński, Przemysław
Brissett, Nigel C.
Bianchi, Julie
Brzostek, Anna
Korycka-Machała, Małgorzata
Dziembowski, Andrzej
Dziadek, Jarosław
Doherty, Aidan J.
author_facet Płociński, Przemysław
Brissett, Nigel C.
Bianchi, Julie
Brzostek, Anna
Korycka-Machała, Małgorzata
Dziembowski, Andrzej
Dziadek, Jarosław
Doherty, Aidan J.
author_sort Płociński, Przemysław
collection PubMed
description 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.
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spelling pubmed-56639582017-11-02 DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria Płociński, Przemysław Brissett, Nigel C. Bianchi, Julie Brzostek, Anna Korycka-Machała, Małgorzata Dziembowski, Andrzej Dziadek, Jarosław Doherty, Aidan J. Nat Commun Article 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. Nature Publishing Group UK 2017-11-01 /pmc/articles/PMC5663958/ /pubmed/29089537 http://dx.doi.org/10.1038/s41467-017-01365-y Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Płociński, Przemysław
Brissett, Nigel C.
Bianchi, Julie
Brzostek, Anna
Korycka-Machała, Małgorzata
Dziembowski, Andrzej
Dziadek, Jarosław
Doherty, Aidan J.
DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title_full DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title_fullStr DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title_full_unstemmed DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title_short DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria
title_sort dna ligase c and prim-polc participate in base excision repair in mycobacteria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5663958/
https://www.ncbi.nlm.nih.gov/pubmed/29089537
http://dx.doi.org/10.1038/s41467-017-01365-y
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