Inhibitors of DNA Polymerases: Their Selectivity and Mode of Action
The first DNA polymerase in mammalian cells was discovered by Bollum (1958), but only in the last years the existence of multiple forms of DNA polymerases was recognized in these cells. In the recent years, there has been a great interest in the purification and characterization of different eukaryotic DNA polymerases, and to study the functional role(s) of each of these enzymes. The field of DNA polymerases gained an unexpected importance as in 1970, a novel DNA polymerase was discovered as a constituent of retrovirus (Temin and Mizutani, 1970; Baltimore 1970), now known as reverse transcriptase (RT). In addition, several new DNA-polymerizing activities are induced in eukaryotic cells infected with DNA viruses. Another unique enzyme which also exhibits a deoxyribonucleotide polymerizing activity is the terminal deoxyribonucleotidyl transferase (TdT). This enzyme, though a cellular enzyme, is unique in the sense that, so far, only thymus tissue has been shown to contain it. In the strictest sense TdT is not a DNA polymerase as it does not require a template to direct the DNA synthesis; nevertheless, it does catalyze the incorporation of deoxyribonucleotides into DNA and thus we consider it here as one of the DNA synthetic enzymes. Like RT the TdT also merits considerable attention as a biochemical marker’for certain types of leukemias, as will be discussed by Dr. Sarin and Dr. Mertelsmann is this proceeding.
KeywordsReverse Transcriptase Reaction Terminal Transferase Deoxyuridine Triphosphate Polycytidylic Acid Thymidine Triphosphate
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