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Bst polymerase — a humble relative of Taq polymerase Full article

Journal Computational and Structural Biotechnology Journal
ISSN: 2001-0370
Output data Year: 2023, Volume: 21, Pages: 4519-4535 Pages count : 17 DOI: 10.1016/j.csbj.2023.09.008
Tags Bst polymeraseDNA polymeraseProcessivityFidelityStrand displacementSite-directed mutagenesisDirected evolutionFusion proteins
Authors Oskorbin I.P. 1 , Filipenko M.L. 1
Affiliations
1 Laboratory of Pharmacogenomics, Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences (ICBFM SB RAS), 8 Lavrentiev Avenue, Novosibirsk 630090, Russia

Funding (1)

1 МИНИСТЕРСТВО НАУКИ И ВЫСШЕГО ОБРАЗОВАНИЯ РОССИЙСКОЙ ФЕДЕРАЦИИ ПФНИ РФ (2021-2030) 0245-2021-0002

Abstract: 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.
Cite: Oskorbin I.P. , Filipenko M.L.
Bst polymerase — a humble relative of Taq polymerase
Computational and Structural Biotechnology Journal. 2023. V.21. P.4519-4535. DOI: 10.1016/j.csbj.2023.09.008 WOS Scopus PMID OpenAlex
Identifiers:
Web of science: WOS:001082229600001
Scopus: 2-s2.0-85172388627
PMID: 37767105
OpenAlex: W4386629834
Citing:
DB Citing
OpenAlex 29
Scopus 8
Web of science 18
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