Dynamics and selective remodeling of the DNA-binding domains of RPA View Full Text


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Article Info

DATE

2019-02

AUTHORS

Nilisha Pokhrel, Colleen C Caldwell, Elliot I Corless, Emma A Tillison, Joseph Tibbs, Nina Jocic, S M Ali Tabei, Marc S Wold, Maria Spies, Edwin Antony

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. More... »

PAGES

129

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41594-018-0181-y

DOI

http://dx.doi.org/10.1038/s41594-018-0181-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111902358

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30723327


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