Document Type
Article
Language
eng
Publication Date
2-4-2019
Publisher
springer
Source Publication
Natural Structure & Molecular Biology
Source ISSN
1545-9993
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.
Recommended Citation
Pokhrel, Nilisha; Caldwell, Colleen C.; Corless, Elliot I.; Tillison, Emma A.; Tibbs, Joseph; Jocic, Nina; Tabei, S. M. Ali; Wold, Marc S.; Spies, Maria; and Antony, Edwin, "Dynamics and Selective Remodeling of the DNA-binding Domains of RPA" (2019). Biological Sciences Faculty Research and Publications. 735.
https://epublications.marquette.edu/bio_fac/735
Comments
Accepted version. Natural Structure & Molecular Biology, Vol. 26, (February 4, 2019): 129-136. DOI. © 2019 Springer. Used with permission.
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