Switching from high-fidelity replicases to low-fidelity lesion-bypass polymerases.
Replication of damaged DNA often requires a DNA polymerase in addition to the cell's normal replicase. Recent research has begun to shed light on the switch from a high-fidelity replicative polymerase to a low-fidelity translesion polymerase that occurs at a stalled replication fork. A picture is emerging in which eukaryotic replicative clamps are posttranslationally modified by ubiquitination, SUMOylation or phosphorylation. It is believed that such modifications help to regulate the access of translesion polymerases to the nascent primer terminus.
Plosky
Brian S
BS
Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2725, USA.
Woodgate
Roger
R
D004249:DNA Damage; D004260:DNA Repair / Q000502:physiology*; D004261:DNA Replication / Q000502:physiology*; D004259:DNA-Directed DNA Polymerase / Q000502:physiology*; D025842:SUMO-1 Protein / Q000502:physiology; D012568:Schizosaccharomyces / Q000201:enzymology / Q000235:genetics; D025801:Ubiquitin / Q000502:physiology
D025842:SUMO-1 Protein; D025801:Ubiquitin; C023140:DNA replicase; D004259:DNA-Directed DNA Polymerase