Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea
Since hyperthermophilic Archaea (HA) thrive in high-temperature environments, which accelerate the rates of deamination of base in DNA, their genomic stability is facing a severe challenge. Hypoxanthine (Hx) is one of the common deaminated bases in DNA. Generally, replication of Hx in DNA before rep...
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Frontiers Media S.A.
2021-08-01
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2021.736915/full |
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author | Tan Lin Likui Zhang Likui Zhang Mai Wu Donghao Jiang Zheng Li Zhihui Yang |
author_facet | Tan Lin Likui Zhang Likui Zhang Mai Wu Donghao Jiang Zheng Li Zhihui Yang |
author_sort | Tan Lin |
collection | DOAJ |
description | Since hyperthermophilic Archaea (HA) thrive in high-temperature environments, which accelerate the rates of deamination of base in DNA, their genomic stability is facing a severe challenge. Hypoxanthine (Hx) is one of the common deaminated bases in DNA. Generally, replication of Hx in DNA before repaired causes AT → GC mutation. Biochemical data have demonstrated that 3-methyladenine DNA glycosylase II (AlkA) and Family V uracil DNA glycosylase (UDG) from HA could excise Hx from DNA, thus triggering a base excision repair (BER) process for Hx repair. Besides, three endonucleases have been reported from HA: Endonuclease V (EndoV), Endonuclease Q (EndoQ), and Endonuclease NucS (EndoNucS), capable of cleaving Hx-containing DNA, thereby providing alternative pathways for Hx repair. Both EndoV and EndoQ could cleave one DNA strand with Hx, thus forming a nick and further initiating an alternative excision repair (AER) process for the follow-up repair. By comparison, EndoNucS cleaves both strands of Hx-containing DNA in a restriction endonuclease manner, thus producing a double-stranded break (DSB). This created DSB might be repaired by homologous recombination (HR) or by a combination activity of DNA polymerase (DNA pol), flap endonuclease 1 (FEN1), and DNA ligase (DNA lig). Herein, we reviewed the most recent advances in repair of Hx in DNA triggered by DNA glycosylases and endonucleases from HA, and proposed future research directions. |
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issn | 1664-302X |
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last_indexed | 2024-12-21T19:20:14Z |
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spelling | doaj.art-e91a361401624b8c907b46472ebfbbb52022-12-21T18:52:58ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-08-011210.3389/fmicb.2021.736915736915Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic ArchaeaTan Lin0Likui Zhang1Likui Zhang2Mai Wu3Donghao Jiang4Zheng Li5Zhihui Yang6College of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, ChinaCollege of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, ChinaGuangling College, Yangzhou University, Yangzhou, ChinaCollege of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, ChinaCollege of Environmental Science and Engineering, Marine Science and Technology Institute, Yangzhou University, Yangzhou, ChinaCollege of Plant Protection, Agricultural University of Hebei, Baoding, ChinaCollege of Plant Protection, Agricultural University of Hebei, Baoding, ChinaSince hyperthermophilic Archaea (HA) thrive in high-temperature environments, which accelerate the rates of deamination of base in DNA, their genomic stability is facing a severe challenge. Hypoxanthine (Hx) is one of the common deaminated bases in DNA. Generally, replication of Hx in DNA before repaired causes AT → GC mutation. Biochemical data have demonstrated that 3-methyladenine DNA glycosylase II (AlkA) and Family V uracil DNA glycosylase (UDG) from HA could excise Hx from DNA, thus triggering a base excision repair (BER) process for Hx repair. Besides, three endonucleases have been reported from HA: Endonuclease V (EndoV), Endonuclease Q (EndoQ), and Endonuclease NucS (EndoNucS), capable of cleaving Hx-containing DNA, thereby providing alternative pathways for Hx repair. Both EndoV and EndoQ could cleave one DNA strand with Hx, thus forming a nick and further initiating an alternative excision repair (AER) process for the follow-up repair. By comparison, EndoNucS cleaves both strands of Hx-containing DNA in a restriction endonuclease manner, thus producing a double-stranded break (DSB). This created DSB might be repaired by homologous recombination (HR) or by a combination activity of DNA polymerase (DNA pol), flap endonuclease 1 (FEN1), and DNA ligase (DNA lig). Herein, we reviewed the most recent advances in repair of Hx in DNA triggered by DNA glycosylases and endonucleases from HA, and proposed future research directions.https://www.frontiersin.org/articles/10.3389/fmicb.2021.736915/fullhyperthermophilic archaeaDNA glycosylaseendonucleasehypoxanthinebase deamination |
spellingShingle | Tan Lin Likui Zhang Likui Zhang Mai Wu Donghao Jiang Zheng Li Zhihui Yang Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea Frontiers in Microbiology hyperthermophilic archaea DNA glycosylase endonuclease hypoxanthine base deamination |
title | Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea |
title_full | Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea |
title_fullStr | Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea |
title_full_unstemmed | Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea |
title_short | Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea |
title_sort | repair of hypoxanthine in dna revealed by dna glycosylases and endonucleases from hyperthermophilic archaea |
topic | hyperthermophilic archaea DNA glycosylase endonuclease hypoxanthine base deamination |
url | https://www.frontiersin.org/articles/10.3389/fmicb.2021.736915/full |
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