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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...

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Autores principales: Shi, Jingru, Oger, Philippe M., Cao, Peng, Zhang, Likui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
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.
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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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