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Nucleic Acids Research, 2000, Vol. 28, No. 5 1276-1281
© 2000 Oxford University Press

Terminal deoxynucleotidyl transferase catalyzes the reaction of DNA phosphorylation

Andrey A. Arzumanov1, Lyubov S. Victorova1,2,*, Maxim V. Jasko1, Dmitry S. Yesipov3 and Alexander A. Krayevsky1

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Street, Moscow 117984, Russia, 2Centre for Medical Studies of University of Oslo, 32 Vavilov Street, Moscow 117984, Russia and 3Moscow State University, Interfaculty Laboratory, Vorob’evy Gory, Moscow 119899, Russia

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 P{alpha}-, P{alpha},{gamma}- or P{alpha},ß,{gamma}-residues served as low-molecular weight substrates. The reaction was TDT specific; human DNA polymerases {alpha} and ß, 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.

* To whom correspondence should be addressed at: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Street, Moscow 117984, Russia. Tel: +7 095 135 2255; Fax: +7 095 135 1405; Email: aak@imb.imb.ac.ru Present address: Andrey A. Arzumanov, PNAC Division, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK


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