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Thermostable DNA ligases from hyperthermophiles in biotechnology
DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo. In vitro, DNA ligase is also used in biotechnological applications requiring in DNA manipulation, including molec...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10244674/ https://www.ncbi.nlm.nih.gov/pubmed/37293226 http://dx.doi.org/10.3389/fmicb.2023.1198784 |
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author | Shi, Jingru Oger, Philippe M. Cao, Peng Zhang, Likui |
author_facet | Shi, Jingru Oger, Philippe M. Cao, Peng Zhang, Likui |
author_sort | Shi, Jingru |
collection | PubMed |
description | DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo. In vitro, DNA ligase is also used in biotechnological applications requiring in DNA manipulation, including molecular cloning, mutation detection, DNA assembly, DNA sequencing, and other aspects. Thermophilic and thermostable enzymes from hyperthermophiles that thrive in the high-temperature (above 80°C) environments have provided an important pool of useful enzymes as biotechnological reagents. Similar to other organisms, each hyperthermophile harbors at least one DNA ligase. In this review, we summarize recent progress on structural and biochemical properties of thermostable DNA ligases from hyperthermophiles, focusing on similarities and differences between DNA ligases from hyperthermophilic bacteria and archaea, and between these thermostable DNA ligases and non-thermostable homologs. Additionally, altered thermostable DNA ligases are discussed. Possessing improved fidelity or thermostability compared to the wild-type enzymes, they could be potential DNA ligases for biotechnology in the future. Importantly, we also describe current applications of thermostable DNA ligases from hyperthermophiles in biotechnology. |
format | Online Article Text |
id | pubmed-10244674 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-102446742023-06-08 Thermostable DNA ligases from hyperthermophiles in biotechnology Shi, Jingru Oger, Philippe M. Cao, Peng Zhang, Likui Front Microbiol Microbiology DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo. In vitro, DNA ligase is also used in biotechnological applications requiring in DNA manipulation, including molecular cloning, mutation detection, DNA assembly, DNA sequencing, and other aspects. Thermophilic and thermostable enzymes from hyperthermophiles that thrive in the high-temperature (above 80°C) environments have provided an important pool of useful enzymes as biotechnological reagents. Similar to other organisms, each hyperthermophile harbors at least one DNA ligase. In this review, we summarize recent progress on structural and biochemical properties of thermostable DNA ligases from hyperthermophiles, focusing on similarities and differences between DNA ligases from hyperthermophilic bacteria and archaea, and between these thermostable DNA ligases and non-thermostable homologs. Additionally, altered thermostable DNA ligases are discussed. Possessing improved fidelity or thermostability compared to the wild-type enzymes, they could be potential DNA ligases for biotechnology in the future. Importantly, we also describe current applications of thermostable DNA ligases from hyperthermophiles in biotechnology. Frontiers Media S.A. 2023-05-24 /pmc/articles/PMC10244674/ /pubmed/37293226 http://dx.doi.org/10.3389/fmicb.2023.1198784 Text en Copyright © 2023 Shi, Oger, Cao and Zhang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Shi, Jingru Oger, Philippe M. Cao, Peng Zhang, Likui Thermostable DNA ligases from hyperthermophiles in biotechnology |
title | Thermostable DNA ligases from hyperthermophiles in biotechnology |
title_full | Thermostable DNA ligases from hyperthermophiles in biotechnology |
title_fullStr | Thermostable DNA ligases from hyperthermophiles in biotechnology |
title_full_unstemmed | Thermostable DNA ligases from hyperthermophiles in biotechnology |
title_short | Thermostable DNA ligases from hyperthermophiles in biotechnology |
title_sort | thermostable dna ligases from hyperthermophiles in biotechnology |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10244674/ https://www.ncbi.nlm.nih.gov/pubmed/37293226 http://dx.doi.org/10.3389/fmicb.2023.1198784 |
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