PMID: 6986914Feb 29, 1980Paper

A study of substrate specificity of mammalian and bacterial DNA polymerases with 5-alkyl-2'-deoxyuridine 5'-triphosphates

Biochimica Et Biophysica Acta
J SágiL Otvös

Abstract

DNA polymerases from procaryotic sources can utilize a variety of dTTP analogues as substrates. We studied here in vitro DNA syntheses catalyzed by DNA polymerase alpha and beta of calf thymus, and for comparison, by the Escherichia coli DNA polymerase I large fragment enzyme in the presence of 5-alkyl derivatives of dUTP as dTTP substrate analogues, using activated DNA as template-primer. The alkyl substituents were n-alkyl (from ethyl to hexyl) and iso-alkyl (isopropyl and tert-butyl) groups. All enzymes were active in the presence of each modified dTTP, incorporation rates of [3H]dAMP or [3H]dGMP were, however, much lower with the analogues than with dTTP. According to relative incorporation rates, alpha-polymerase in DNA synthesis was found to be less sensitive to changes in the length of the alkyl substituent of 5-n-alkyl-dUTPs than beta-polymerase or the E. coli enzyme. Evidence for the incorporation of the analogues was presented for 5-[2-14C]isopropyl-dUTP.

References

Feb 27, 1979·Biochimica Et Biophysica Acta·D K DubeL A Loeb
Aug 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·R M DaleD C Ward
Jan 1, 1974·Methods in Enzymology·F J BollumJ W Dorson
Jan 1, 1970·Albrecht Von Graefes Archiv Für Klinische Und Experimentelle Ophthalmologie. Albrecht Von Graefe's Archive for Clinical and Experimental Ophthalmology·K K GauriE Riehm
Apr 1, 1964·Journal of Molecular Biology·R B INMAN, R L BALDWIN
Jul 15, 1958·Proceedings of the National Academy of Sciences of the United States of America·M J BessmanA Kornberg

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