Conformational changes during nucleotide selection by Sulfolobus solfataricus DNA polymerase Dpo4.

ABSTRACT: The mechanism of nucleotide selection by Y-family DNA polymerases has been the subject of intense study, but significant structural contacts and/or conformational changes that relate to polymerase fidelity have been difficult to identify. Here we report on the conformational dynamics of a model Y-family polymerase Dpo4 from Sulfolobus solfataricus. Hydrogen-deuterium exchange in tandem with mass spectrometry was used to monitor changes in Dpo4 structure as a function of time and the presence or absence of specific substrates and ligands. Analysis of the data revealed previously unrecognized structural changes that accompany steps in the catalytic cycle leading up to phosphoryl transfer. For example, the solvent accessibility of the alphaB-loop-alphaC region in the finger domain decreased i

SUBMITTER: Eoff RL 

PROVIDER: S-EPMC2742873 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature