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However, these mutagenic effects are inhibited when the phage's DNA synthesis is catalyzed by the tsCB120 antimutator polymerase, or another antimutator polymerase, tsCB87. [9] These findings indicate that the level of induction of mutations by DNA damage can be strongly influenced by the gene 43 DNA polymerase proofreading function.
DNA polymerase's ability to slide along the DNA template allows increased processivity. There is a dramatic increase in processivity at the replication fork. This increase is facilitated by the DNA polymerase's association with proteins known as the sliding DNA clamp. The clamps are multiple protein subunits associated in the shape of a ring.
Base excision repair (BER) of oxidative damage occurred with the DNA repair enzyme polymerase beta localizing to oxidized guanines. Polymerase beta is the main human polymerase in short-patch BER of oxidative DNA damage. Jiang et al. [144] also found that polymerase beta recruited the DNA methyltransferase protein DNMT3b
DNA mismatch repair (MMR) is a system for recognizing and repairing erroneous insertion, deletion, and mis-incorporation of bases that can arise during DNA replication and recombination, as well as repairing some forms of DNA damage.
DNA damage recognition and repair – a certain DNA repair mechanism utilizes kinetic proofreading to discriminate damaged DNA. [8] Some DNA polymerases can also detect when they have added an incorrect base and are able to hydrolyze it immediately; in this case, the irreversible (energy-requiring) step is addition of the base.
After this, Rad51 replaces RPA and forms filaments on the DNA strand. Working together with BRCA2 (Breast Cancer Associated), Rad51 couples a complementary DNA piece which invades the broken DNA strand to form a template for the polymerase. The polymerase is held onto the DNA strand by PCNA (Proliferating Cell Nuclear Antigen). PCNA forms ...