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Bst polymerase — a humble relative of Taq polymerase

DNA polymerases are a superfamily of enzymes synthesizing DNA using DNA as a template. They are essential for nucleic acid metabolism and for DNA replication and repair. Modern biotechnology and molecular diagnostics rely heavily on DNA polymerases in analyzing nucleic acids. Among a variety of disc...

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Detalles Bibliográficos
Autores principales: Oscorbin, Igor, Filipenko, Maxim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520511/
https://www.ncbi.nlm.nih.gov/pubmed/37767105
http://dx.doi.org/10.1016/j.csbj.2023.09.008
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author Oscorbin, Igor
Filipenko, Maxim
author_facet Oscorbin, Igor
Filipenko, Maxim
author_sort Oscorbin, Igor
collection PubMed
description DNA polymerases are a superfamily of enzymes synthesizing DNA using DNA as a template. They are essential for nucleic acid metabolism and for DNA replication and repair. Modern biotechnology and molecular diagnostics rely heavily on DNA polymerases in analyzing nucleic acids. Among a variety of discovered DNA polymerases, Bst polymerase, a large fragment of DNA polymerase I from Geobacillus stearothermophilus, is one of the most commonly used but is not as well studied as Taq polymerase. The ability of Bst polymerase to displace an upstream DNA strand during synthesis, coupled with its moderate thermal stability, has provided the basis for several isothermal DNA amplification methods, including LAMP, WGA, RCA, and many others. Bst polymerase is one of the key components defining the robustness and analytical characteristics of diagnostic test systems based on isothermal amplification. Here, we present an overview of the biochemical and structural features of Bst polymerase and provide information on its mutated analogs.
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spelling pubmed-105205112023-09-27 Bst polymerase — a humble relative of Taq polymerase Oscorbin, Igor Filipenko, Maxim Comput Struct Biotechnol J Review Article DNA polymerases are a superfamily of enzymes synthesizing DNA using DNA as a template. They are essential for nucleic acid metabolism and for DNA replication and repair. Modern biotechnology and molecular diagnostics rely heavily on DNA polymerases in analyzing nucleic acids. Among a variety of discovered DNA polymerases, Bst polymerase, a large fragment of DNA polymerase I from Geobacillus stearothermophilus, is one of the most commonly used but is not as well studied as Taq polymerase. The ability of Bst polymerase to displace an upstream DNA strand during synthesis, coupled with its moderate thermal stability, has provided the basis for several isothermal DNA amplification methods, including LAMP, WGA, RCA, and many others. Bst polymerase is one of the key components defining the robustness and analytical characteristics of diagnostic test systems based on isothermal amplification. Here, we present an overview of the biochemical and structural features of Bst polymerase and provide information on its mutated analogs. Research Network of Computational and Structural Biotechnology 2023-09-12 /pmc/articles/PMC10520511/ /pubmed/37767105 http://dx.doi.org/10.1016/j.csbj.2023.09.008 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review Article
Oscorbin, Igor
Filipenko, Maxim
Bst polymerase — a humble relative of Taq polymerase
title Bst polymerase — a humble relative of Taq polymerase
title_full Bst polymerase — a humble relative of Taq polymerase
title_fullStr Bst polymerase — a humble relative of Taq polymerase
title_full_unstemmed Bst polymerase — a humble relative of Taq polymerase
title_short Bst polymerase — a humble relative of Taq polymerase
title_sort bst polymerase — a humble relative of taq polymerase
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520511/
https://www.ncbi.nlm.nih.gov/pubmed/37767105
http://dx.doi.org/10.1016/j.csbj.2023.09.008
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