Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase.

ABSTRACT: DNA-binding proteins utilise different recognition mechanisms to locate their DNA targets; some proteins recognise specific DNA sequences, while others interact with specific DNA structures. While sequence-specific DNA binding has been studied extensively, structure-specific recognition mechanisms remain unclear. Here, we study structure-specific DNA recognition by examining the structure and dynamics of DNA polymerase I Klenow Fragment (Pol) substrates both alone and in DNA-Pol complexes. Using a docking approach based on a network of 73 distances collected using single-molecule FRET, we determined a novel solution structure of the single-nucleotide-gapped DNA-Pol binary complex. The structure resembled existing crystal structures with regards to the downstream primer-template DNA substra

SUBMITTER: Craggs TD 

PROVIDER: S-EPMC6846080 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature