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- W2076834982 abstract "Recent data suggest that DNA polymerases α and δ might have a coordinate functional role at the replication fork. In this communication we show that Mg2+ is likely the natural metal activator for both enzymes. Mn2+, a known mutagenic agent, is a competitive inhibitor of Mg2+ for DNA polymerase δ and acompetitive for DNA polymerase α. The 3'→ 5' exonuclease activity associated with DNA polymerase δ is not affected upon addition of Mn2+, Be2+, another mutagenic agent, on the other hand, has an inhibitory effect on the 3' → 5' exonuclease, but not on the DNA polymerase δ. The data presented might explain the mutagenic and carcinogenic potential of these two divalent cations." @default.
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- W2076834982 date "1990-01-01" @default.
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- W2076834982 title "Effect of divalent and monovalent cations on calf thymus PCNA-independent DNA polymerase δ and its 3' → 5' exonuclease" @default.
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- W2076834982 doi "https://doi.org/10.1016/0014-5793(90)80045-k" @default.
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