Investigation of Intradomain Motions of a Y-Family DNA Polymerase during Substrate Binding and Catalysis.

ABSTRACT: DNA polymerases catalyze DNA synthesis through a stepwise kinetic mechanism that begins with binding to DNA, followed by selection, binding, and incorporation of a nucleotide into an elongating primer. It is hypothesized that subtle active site adjustments in a polymerase to align reactive moieties limit the rate of correct nucleotide incorporation. DNA damage can impede this process for many DNA polymerases, causing replication fork stalling, genetic mutations, and potentially cell death. However, specialized Y-family DNA polymerases are structurally evolved to efficiently bypass DNA damage in vivo, albeit at the expense of replication fidelity. Dpo4, a model Y-family polymerase from Sulfolobus solfataricus, has been well-studied kinetically, structurally, and computationally, which yield

SUBMITTER: Raper AT 

PROVIDER: S-EPMC8225418 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature