DNA replication is fast and highly efficient due to the polymerases that carry out this process. DNA Polymerase III (Pol III) is the main replicative polymerase of E. coli composed of over 10 proteins. A subset of these proteins, termed Pol III*, includes the polymerase and exonuclease domains α and ε, the clamp, β, and an accessory protein θ. Previous work has shown that a single mutation in the α subunit can impact the proofreading activity carried out by the exonuclease, ε (PCCP. 20, 26892-26902). In a separate work, it has previously been reported that the L82E and L82D mutations on both monomers of the β dimer cause a destabilization of this subunit (Biophys. J. 117, 587-601). We will present results for the molecular dynamics simulation of the whole complex of E. coli Pol III* wildtype, β L82E, and β L82D. These results provide insights into the effects of the mutations on the β clamp and the proofreading activity of ε.

Molecular dynamics investigation on the effects of distal mutations on DNA polymerase III*

ACS Spring Meeting 2021

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