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Maxim V. Jasko - One of the best experts on this subject based on the ideXlab platform.

  • New nonnucleoside substrates for Terminal Deoxynucleotidyl Transferase: Synthesis and dependence of substrate properties on structure
    Russian Journal of Bioorganic Chemistry, 2005
    Co-Authors: Anastasiya L. Khandazhinskaya, Marina K. Kukhanova, Maxim V. Jasko
    Abstract:

    N-(9-Fluorenylmethoxycarbonyl)-ω-aminoalkyl-, N-(9-fluorenylmethoxycarbonyl)-8-amino-3,6-dioxaoctyl, and N-[(9-fluorenylmethoxycarbonyl)-6-aminohexanoyl]-2-aminoethyl triphosphates were synthesized. All of them were shown to be the substrates of the calf thymus Terminal Deoxynucleotidyl Transferase. Their substrate properties depend on the length and structure of the linker between the 9-fluorenylmethoxycarbonyl and triphosphate moieties.

  • Terminal Deoxynucleotidyl Transferase catalyzes the reaction of DNA phosphorylation
    Nucleic acids research, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko, Dmitry S. Yesipov, Alexander A. Krayevsky
    Abstract:

    The reaction of phosphorylation and phosphonylation of an oligodeoxynucleotide 3'-Terminal hydroxyl (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) was found. Triphosphates modified at Palpha-, Palpha,gamma- or Palpha,beta,gamma-residues served as low-molecular weight substrates. The reaction was TDT specific; human DNA polymerasesalphaandbeta, as well as AMV reverse transcriptase did not catalyze it. The donor activity of modified triphosphates or triphosphonates depended on their structure and was increased with an increase in their hydrophobicity. The substrate activity of some modified triphosphates was up to one order of magnitude higher than that of ddTTP.

  • Terminal Deoxynucleotidyl Transferase: catalysis of DNA (oligodeoxynucleotide) phosphorylation
    Pharmacology & therapeutics, 2000
    Co-Authors: Alexander A. Krayevsky, Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract The phosphorylation and phosphonylation of the 3′-hydroxyl of oligodeoxynucleotide 3′-termini (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) are discussed. Pα and Pα,Pγ-substituted modified triphosphates serve as low-molecular weight substrates in this reaction to give oligodeoxynucleotides with a 3′-phosphorylated or phosphonylated hydroxyl. The reaction is specific for TDT, and it is not catalyzed by avian myeloblastosis virus reverse transcriptase. The phosphate or phosphonate donor activities of modified triphosphates depend on their structure and increase with hydrophobicity. Several modified triphosphates demonstrated very high substrate activity, in some cases, up to one order of magnitude higher than that for dTTP. It has also been shown that TDT catalyzes primer extension with dinucleoside 5′,5′-tetraphosphates as substrates.

  • Synthesis of non-nucleoside triphosphate analogues, a new type of substrates for Terminal Deoxynucleotidyl Transferase.
    Nucleosides nucleotides & nucleic acids, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract A series of non-nucleoside triphosphate analogues were synthesized. In place of the nucleoside fragment, substituents bearing aromatic groups were introduced; the triphosphate component was replaced at α, β, or γ-positions by phosphonates. α-[2-N-(9-Fluorenylmethoxycarbonyl)aminoethylphosphonyl]-β,γ-difluoromethylenediphosphonate (IIc) revealed the best substrate properties toward Terminal Deoxynucleotidyl Transferase.

Alexander A. Krayevsky - One of the best experts on this subject based on the ideXlab platform.

  • Terminal Deoxynucleotidyl Transferase catalyzes the reaction of DNA phosphorylation
    Nucleic acids research, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko, Dmitry S. Yesipov, Alexander A. Krayevsky
    Abstract:

    The reaction of phosphorylation and phosphonylation of an oligodeoxynucleotide 3'-Terminal hydroxyl (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) was found. Triphosphates modified at Palpha-, Palpha,gamma- or Palpha,beta,gamma-residues served as low-molecular weight substrates. The reaction was TDT specific; human DNA polymerasesalphaandbeta, as well as AMV reverse transcriptase did not catalyze it. The donor activity of modified triphosphates or triphosphonates depended on their structure and was increased with an increase in their hydrophobicity. The substrate activity of some modified triphosphates was up to one order of magnitude higher than that of ddTTP.

  • Terminal Deoxynucleotidyl Transferase: catalysis of DNA (oligodeoxynucleotide) phosphorylation
    Pharmacology & therapeutics, 2000
    Co-Authors: Alexander A. Krayevsky, Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract The phosphorylation and phosphonylation of the 3′-hydroxyl of oligodeoxynucleotide 3′-termini (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) are discussed. Pα and Pα,Pγ-substituted modified triphosphates serve as low-molecular weight substrates in this reaction to give oligodeoxynucleotides with a 3′-phosphorylated or phosphonylated hydroxyl. The reaction is specific for TDT, and it is not catalyzed by avian myeloblastosis virus reverse transcriptase. The phosphate or phosphonate donor activities of modified triphosphates depend on their structure and increase with hydrophobicity. Several modified triphosphates demonstrated very high substrate activity, in some cases, up to one order of magnitude higher than that for dTTP. It has also been shown that TDT catalyzes primer extension with dinucleoside 5′,5′-tetraphosphates as substrates.

Anthony J. Berdis - One of the best experts on this subject based on the ideXlab platform.

  • Terminal Deoxynucleotidyl Transferase: The Story of A Misguided DNA Polymerase
    Biochimica et biophysica acta, 2009
    Co-Authors: Edward A. Motea, Anthony J. Berdis
    Abstract:

    Nearly every DNA polymerase characterized to date exclusively catalyzes the incorporation of mononucleotides into a growing primer using a DNA or RNA template as a guide to direct each incorporation event. There is, however, one unique DNA polymerase designated Terminal Deoxynucleotidyl Transferase that performs DNA synthesis using only single-stranded DNA as the nucleic acid substrate. In this chapter, we review the biological role of this enigmatic DNA polymerase and the biochemical mechanism for its ability to perform DNA synthesis in the absence of a templating strand. We compare and contrast the molecular events for template-independent DNA synthesis catalyzed by Terminal Deoxynucleotidyl Transferase with other well-characterized DNA polymerases that perform template-dependent synthesis. This includes a quantitative inspection of how Terminal Deoxynucleotidyl Transferase binds DNA and dNTP substrates, the possible involvement of a conformational change that precedes phosphoryl transfer, and kinetic steps that are associated with the release of products. These enzymatic steps are discussed within the context of the available structures of Terminal Deoxynucleotidyl Transferase in the presence of DNA or nucleotide substrate. In addition, we discuss the ability of proteins involved in replication and recombination to regulate the activity of the Terminal Deoxynucleotidyl Transferase. Finally, the biomedical role of this specialized DNA polymerase is discussed focusing on its involvement in cancer development and its use in biomedical applications such as labeling DNA for detecting apoptosis.

Andrey A. Arzumanov - One of the best experts on this subject based on the ideXlab platform.

  • Terminal Deoxynucleotidyl Transferase catalyzes the reaction of DNA phosphorylation
    Nucleic acids research, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko, Dmitry S. Yesipov, Alexander A. Krayevsky
    Abstract:

    The reaction of phosphorylation and phosphonylation of an oligodeoxynucleotide 3'-Terminal hydroxyl (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) was found. Triphosphates modified at Palpha-, Palpha,gamma- or Palpha,beta,gamma-residues served as low-molecular weight substrates. The reaction was TDT specific; human DNA polymerasesalphaandbeta, as well as AMV reverse transcriptase did not catalyze it. The donor activity of modified triphosphates or triphosphonates depended on their structure and was increased with an increase in their hydrophobicity. The substrate activity of some modified triphosphates was up to one order of magnitude higher than that of ddTTP.

  • Terminal Deoxynucleotidyl Transferase: catalysis of DNA (oligodeoxynucleotide) phosphorylation
    Pharmacology & therapeutics, 2000
    Co-Authors: Alexander A. Krayevsky, Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract The phosphorylation and phosphonylation of the 3′-hydroxyl of oligodeoxynucleotide 3′-termini (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) are discussed. Pα and Pα,Pγ-substituted modified triphosphates serve as low-molecular weight substrates in this reaction to give oligodeoxynucleotides with a 3′-phosphorylated or phosphonylated hydroxyl. The reaction is specific for TDT, and it is not catalyzed by avian myeloblastosis virus reverse transcriptase. The phosphate or phosphonate donor activities of modified triphosphates depend on their structure and increase with hydrophobicity. Several modified triphosphates demonstrated very high substrate activity, in some cases, up to one order of magnitude higher than that for dTTP. It has also been shown that TDT catalyzes primer extension with dinucleoside 5′,5′-tetraphosphates as substrates.

  • Synthesis of non-nucleoside triphosphate analogues, a new type of substrates for Terminal Deoxynucleotidyl Transferase.
    Nucleosides nucleotides & nucleic acids, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract A series of non-nucleoside triphosphate analogues were synthesized. In place of the nucleoside fragment, substituents bearing aromatic groups were introduced; the triphosphate component was replaced at α, β, or γ-positions by phosphonates. α-[2-N-(9-Fluorenylmethoxycarbonyl)aminoethylphosphonyl]-β,γ-difluoromethylenediphosphonate (IIc) revealed the best substrate properties toward Terminal Deoxynucleotidyl Transferase.

Lyubov S. Victorova - One of the best experts on this subject based on the ideXlab platform.

  • Terminal Deoxynucleotidyl Transferase catalyzes the reaction of DNA phosphorylation
    Nucleic acids research, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko, Dmitry S. Yesipov, Alexander A. Krayevsky
    Abstract:

    The reaction of phosphorylation and phosphonylation of an oligodeoxynucleotide 3'-Terminal hydroxyl (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) was found. Triphosphates modified at Palpha-, Palpha,gamma- or Palpha,beta,gamma-residues served as low-molecular weight substrates. The reaction was TDT specific; human DNA polymerasesalphaandbeta, as well as AMV reverse transcriptase did not catalyze it. The donor activity of modified triphosphates or triphosphonates depended on their structure and was increased with an increase in their hydrophobicity. The substrate activity of some modified triphosphates was up to one order of magnitude higher than that of ddTTP.

  • Terminal Deoxynucleotidyl Transferase: catalysis of DNA (oligodeoxynucleotide) phosphorylation
    Pharmacology & therapeutics, 2000
    Co-Authors: Alexander A. Krayevsky, Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract The phosphorylation and phosphonylation of the 3′-hydroxyl of oligodeoxynucleotide 3′-termini (oligoDeoxynucleotidyl kinase activity) catalyzed by calf thymus Terminal Deoxynucleotidyl Transferase (TDT) are discussed. Pα and Pα,Pγ-substituted modified triphosphates serve as low-molecular weight substrates in this reaction to give oligodeoxynucleotides with a 3′-phosphorylated or phosphonylated hydroxyl. The reaction is specific for TDT, and it is not catalyzed by avian myeloblastosis virus reverse transcriptase. The phosphate or phosphonate donor activities of modified triphosphates depend on their structure and increase with hydrophobicity. Several modified triphosphates demonstrated very high substrate activity, in some cases, up to one order of magnitude higher than that for dTTP. It has also been shown that TDT catalyzes primer extension with dinucleoside 5′,5′-tetraphosphates as substrates.

  • Synthesis of non-nucleoside triphosphate analogues, a new type of substrates for Terminal Deoxynucleotidyl Transferase.
    Nucleosides nucleotides & nucleic acids, 2000
    Co-Authors: Andrey A. Arzumanov, Lyubov S. Victorova, Maxim V. Jasko
    Abstract:

    Abstract A series of non-nucleoside triphosphate analogues were synthesized. In place of the nucleoside fragment, substituents bearing aromatic groups were introduced; the triphosphate component was replaced at α, β, or γ-positions by phosphonates. α-[2-N-(9-Fluorenylmethoxycarbonyl)aminoethylphosphonyl]-β,γ-difluoromethylenediphosphonate (IIc) revealed the best substrate properties toward Terminal Deoxynucleotidyl Transferase.