Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis.

ABSTRACT: DNA polymerase β (pol β) plays a central role in the DNA base excision repair pathway and also serves as an important model polymerase. Dynamic characterization of pol β from methyl-TROSY 13C-1H multiple quantum CPMG relaxation dispersion experiments of Ile and Met sidechains and previous backbone relaxation dispersion measurements, reveals transitions in μs-ms dynamics in response to highly variable substrates. Recognition of a 1-nt-gapped DNA substrate is accompanied by significant backbone and sidechain motion in the lyase domain and the DNA binding subdomain of the polymerase domain, that may help to facilitate binding of the apoenzyme to the segments of the DNA upstream and downstream from the gap. Backbone μs-ms motion largely disappears after formation of the pol β-DNA complex, givi

SUBMITTER: DeRose EF 

PROVIDER: S-EPMC6101544 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature