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In this case, a different exonuclease-proficient DNA polymerase may proofread errors by Y831A Pol ε.
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In addition, the mutation rates of strains with the pol2-4 mutatinn in combination with active site mutator mutations in Pol δ and Pol α suggest that Pol ε may proofread certain errors made by Pol α and Pol δ during replication in vivo.
Moreover, these data also demonstrate that Pol III does not proofread errors made by Pol IV, or any other DNA polymerase generating stress-induced point mutations.
Although errors made by Y831A Pol ε do not appear to be proofread by Pol δ, it is possible that Pol ε might proofread errors by other polymerases.
Conversely, Pol ε can proofread errors made by polymerases α and δ.
Additionally, Pol δ can replace Pol ε to proofread errors created by defective Pol ε and can complete DNA synthesis on the leading strand (Flood et al. 2015).
Like its family X siblings, pol λ is a single-subunit, monomeric enzyme with limited processivity and no intrinsic 3′ → 5′ exonucleolytic activity to proofread errors.
It has been suggested that in yeast, Pol ɛ and Pol δ proofread opposite strands at defined replication origins and may proofread for each other [ 6,18,19].
Reading aloud will also help you catch proofreading errors that need correcting.
Although this excerpt has been proofread, occasional errors may appear due to the scanning process.
In the future, it will be interesting to test this hypothesis further, to determine under what circumstances, for example, translesion DNA synthesis [ 43] or base excision repair [ 44] errors made by one DNA polymerase may be proofread by an exonuclease intrinsic to a second DNA polymerase or even another protein [ 45].
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