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Template specific inhibitor of mammalian DNA polymerases.
Author(s) -
Josef Pitha,
Samuel H. Wilson
Publication year - 1976
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/3.3.825
Subject(s) - biology , dna polymerase , polymerase , primer (cosmetics) , dna , enzyme , dna clamp , dna replication , microbiology and biotechnology , dna polymerase beta , biochemistry , nucleotide , base pair , dna synthesis , dna polymerase i , dna polymerase ii , dna polymerase delta , polymerase chain reaction , reverse transcriptase , dna repair , base excision repair , gene , chemistry , organic chemistry
A study of the inhibition of mouse cellular DNA polymerases by poly-nucleotides and their vinyl analogs is presented. Poly(dT)-directed poly(dA) synthesis by representatives of all three classes of cellular DNA polymerase could be completely inhibited by poly(9-vinyladenine), although higher concentrations were required in the case of the gamma class enzyme. Studies on the mechanism of the inhibition using the alpha class DNA polymerase and different templates showed that the enzyme activity was inhibited in all cases where base-pairing between the vinyl polymer and the template occurred; poly(9-vinyladenine) did not interfere with the replication of templates to which it does not bind. The inhibition occurred shortly after addition of poly(9-vinyladenine) to ongoing reactions, yet the enzyme was not displaced from the template - primer complex.

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