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Effect of divalent and monovalent cations on calf thymus PCNA‐independent DNA polymerase δ and its 3' → 5' exonuclease
Author(s) -
Focher Federico,
Verri Annalisa,
Maga Giovanni,
Spadari Silvio,
Hübscher Ulrich
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80045-k
Subject(s) - dna polymerase , dna polymerase ii , klenow fragment , dna clamp , exonuclease , polymerase , dna polymerase i , dna polymerase delta , dna , chemistry , dna replication , divalent , microbiology and biotechnology , biochemistry , biology , polymerase chain reaction , gene , reverse transcriptase , organic chemistry
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 Mg 2+ is likely the natural metal activator for both enzymes. Mn 2+ , a known mutagenic agent, is a competitive inhibitor of Mg 2+ 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 Mn 2+ , Be 2+ , 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.