Реферат: Terminal deoxynucleotidyltransferase (TdT) is a member of the DNA polymerase X family that is responsible for random addition of nucleotides to single-stranded DNA. We present investigation into the role of metal ions and specific interactions of dNTP with active-site amino acid residues in the mechanisms underlying the recognition of nucleoside triphosphates by human TdT under pre-steady-state conditions. In the elongation mode, the ratios of translocation and dissociation rate constants, as well as the catalytic rate constant were dependent on the nature of the nucleobase. Preferences of TdT in dNTP incorporation were researched by molecular dynamics simulations of complexes of TdT with a primer and dNTP or with the elongated primer. Purine nucleotides lost the summarisedH-bonding network after the attachment of the nucleotide to the primer, whereas pyrimidine nucleotides increased the number and relative lifetime of H-bonds in the post-catalytic complex. The effect of divalent metal ions on the primer elongation revealed that Me2+ cofactor can significantly change parameters of the primer elongation by strongly affecting the rate of nucleotide attachment and the polymerisation mode. © 2022 Kuznetsova et al.

Библиографическая ссылка: Kuznetsova A.A. , Tyugashev T.E. , Alekseeva I.V. , Timofeyeva N.A. , Fedorova O.S. , Kuznetsov N.A.
Insight into the mechanism of DNA synthesis by human terminal deoxynucleotidyltransferase
Life Science Alliance. 2022. V.5. N12. e202201428 . DOI: 10.26508/lsa.202201428 WOS Scopus OpenAlex

Идентификаторы БД:

Web of science:	WOS:000842555300003
Scopus:	2-s2.0-85135306187
OpenAlex:	W4289260498

Цитирование в БД:

БД	Цитирований
Scopus	3
OpenAlex	13
Web of science	11

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