Research output: Contribution to journal › Article › peer-review
Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties. / Bulygin, A. A.; Kuznetsova, A. A.; Fedorova, O. S. et al.
In: Molecular Biology, Vol. 57, No. 2, 04.2023, p. 182-192.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties
AU - Bulygin, A. A.
AU - Kuznetsova, A. A.
AU - Fedorova, O. S.
AU - Kuznetsov, N. A.
N1 - The work was supported by the Ministry of Science and Higher Education, agreement no. 075-15-2021-1085. Публикация для корректировки.
PY - 2023/4
Y1 - 2023/4
N2 - DNA polymerases catalyze DNA synthesis during DNA replication, repair, and recombination. A number of DNA polymerases, such as the Taq enzyme from Thermus aquaticus, are used in various applications of molecular biology and biotechnology, in particular as DNA amplification tools. However, the efficiency of these enzymes depends on factors such as DNA origin, primer composition, template length, GC-content, and the ability to form stable secondary structures. These limitations in the use of currently known DNA polymerases lead to the search for new enzymes with improved properties. This review summarizes the main structural and molecular-kinetic features of the functioning of DNA-polymerases belonging to structural family A, including Taq polymerase. A phylogenetic analysis of these enzymes was carried out, which made it possible to establish a highly conserved consensus sequence containing 62 amino acid residues distributed over the structure of the enzyme. A comparative analysis of these amino acid residues among poorly studied DNA-polymerases revealed 7 enzymes that potentially have the properties necessary for use in DNA amplification.
AB - DNA polymerases catalyze DNA synthesis during DNA replication, repair, and recombination. A number of DNA polymerases, such as the Taq enzyme from Thermus aquaticus, are used in various applications of molecular biology and biotechnology, in particular as DNA amplification tools. However, the efficiency of these enzymes depends on factors such as DNA origin, primer composition, template length, GC-content, and the ability to form stable secondary structures. These limitations in the use of currently known DNA polymerases lead to the search for new enzymes with improved properties. This review summarizes the main structural and molecular-kinetic features of the functioning of DNA-polymerases belonging to structural family A, including Taq polymerase. A phylogenetic analysis of these enzymes was carried out, which made it possible to establish a highly conserved consensus sequence containing 62 amino acid residues distributed over the structure of the enzyme. A comparative analysis of these amino acid residues among poorly studied DNA-polymerases revealed 7 enzymes that potentially have the properties necessary for use in DNA amplification.
KW - DNA-polymerase
KW - active site
KW - catalytic mechanism
KW - kinetics
KW - protein-nucleic acid interactions
KW - structural family
UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85156109967&origin=inward&txGid=902a8ff0fa75bbc648ba96cf3ecca07c
UR - https://www.mendeley.com/catalogue/150d15ec-52ee-3ed4-8c45-176ecb67880e/
U2 - 10.1134/S0026893323020048
DO - 10.1134/S0026893323020048
M3 - Article
VL - 57
SP - 182
EP - 192
JO - Molecular Biology
JF - Molecular Biology
SN - 0026-8933
IS - 2
ER -
ID: 59649353