Faculty Publications

Dynamics And Selective Remodeling Of The DNA-Binding Domains Of RPA

Document Type

Article

Journal/Book/Conference Title

Nature Structural and Molecular Biology

Volume

26

Issue

2

First Page

129

Last Page

136

Abstract

Replication protein A (RPA) coordinates important DNA metabolic events by stabilizing single-stranded DNA (ssDNA) intermediates, activating the DNA-damage response and handing off ssDNA to the appropriate downstream players. Six DNA-binding domains (DBDs) in RPA promote high-affinity binding to ssDNA yet also allow RPA displacement by lower affinity proteins. We generated fluorescent versions of Saccharomyces cerevisiae RPA and visualized the conformational dynamics of individual DBDs in the context of the full-length protein. We show that both DBD-A and DBD-D rapidly bind to and dissociate from ssDNA while RPA remains bound to ssDNA. The recombination mediator protein Rad52 selectively modulates the dynamics of DBD-D. These findings reveal how RPA-interacting proteins with lower ssDNA binding affinities can access the occluded ssDNA and remodel individual DBDs to replace RPA.

Department

Department of Physics

Original Publication Date

2-1-2019

DOI of published version

10.1038/s41594-018-0181-y

Repository

UNI ScholarWorks, Rod Library, University of Northern Iowa

Language

en

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