TY - JOUR
T1 - Eukaryotic DNA polymerases in DNA replication and DNA repair
AU - Burgers, Peter M.J.
N1 - Funding Information:
Acknowledgements. The work in the author’s laboratory is supported in part by Grant GM32431 from the National Institutes of Health.
PY - 1998
Y1 - 1998
N2 - DNA polymerases carry out a large variety of synthetic transactions during DNA replication, DNA recombination and DNA repair. Substrates for DNA polymerases vary from single nucleotide gaps to kilobase size gaps and from relatively simple gapped structures to complex replication forks in which two strands need to be replicated simultaneously. Consequently, one would expect the cell to have developed a well-defined set of DNA polymerases with each one uniquely adapted for a specific pathway. And to some degree this turns out to be the case. However, in addition we seem to find a large degree of cross-functionality of DNA polymerases in these different pathways. DNA polymerase α is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role beyond that of checkpoint control has been assigned to this enzyme. DNA polymerase δ functions as a dimer and, therefore, may be responsible for both leading and lagging strand DNA replication. In addition, this enzyme is required for mismatch repair and, together with DNA polymerase ζ, for mutagenesis. The function of DNA polymerase ε in DNA replication may be restricted to that of Okazaki fragment maturation. In contrast, either polymerase δ or ε suffices for the repair of UV induced damage. The role of DNA polymerase β in base-excision repair is well established for mammalian systems, but in yeast, DNA polymerase δ appears to fullfill that function.
AB - DNA polymerases carry out a large variety of synthetic transactions during DNA replication, DNA recombination and DNA repair. Substrates for DNA polymerases vary from single nucleotide gaps to kilobase size gaps and from relatively simple gapped structures to complex replication forks in which two strands need to be replicated simultaneously. Consequently, one would expect the cell to have developed a well-defined set of DNA polymerases with each one uniquely adapted for a specific pathway. And to some degree this turns out to be the case. However, in addition we seem to find a large degree of cross-functionality of DNA polymerases in these different pathways. DNA polymerase α is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role beyond that of checkpoint control has been assigned to this enzyme. DNA polymerase δ functions as a dimer and, therefore, may be responsible for both leading and lagging strand DNA replication. In addition, this enzyme is required for mismatch repair and, together with DNA polymerase ζ, for mutagenesis. The function of DNA polymerase ε in DNA replication may be restricted to that of Okazaki fragment maturation. In contrast, either polymerase δ or ε suffices for the repair of UV induced damage. The role of DNA polymerase β in base-excision repair is well established for mammalian systems, but in yeast, DNA polymerase δ appears to fullfill that function.
UR - https://www.scopus.com/pages/publications/0031686246
U2 - 10.1007/s004120050300
DO - 10.1007/s004120050300
M3 - Review article
C2 - 9745046
AN - SCOPUS:0031686246
SN - 0009-5915
VL - 107
SP - 218
EP - 227
JO - Chromosoma
JF - Chromosoma
IS - 4
ER -