Document Type
Article
Language
eng
Publication Date
12-21-2018
Publisher
Springer Nature Publishing
Source Publication
Nature Communications
Source ISSN
2041-1723
Abstract
Replication Protein A (RPA), the major eukaryotic single stranded DNA-binding protein, binds to exposed ssDNA to protect it from nucleases, participates in a myriad of nucleic acid transactions and coordinates the recruitment of other important players. RPA is a heterotrimer and coats long stretches of single-stranded DNA (ssDNA). The precise molecular architecture of the RPA subunits and its DNA binding domains (DBDs) during assembly is poorly understood. Using cryo electron microscopy we obtained a 3D reconstruction of the RPA trimerisation core bound with ssDNA (∼55 kDa) at ∼4.7 Å resolution and a dimeric RPA assembly on ssDNA. FRET-based solution studies reveal dynamic rearrangements of DBDs during coordinated RPA binding and this activity is regulated by phosphorylation at S178 in RPA70. We present a structural model on how dynamic DBDs promote the cooperative assembly of multiple RPAs on long ssDNA.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Yates, Luke A.; Aramayo, Ricardo J.; Pokhrel, Nilisha; Caldwell, Colleen C.; Kaplan, Joshua A.; Perera, Rajika L.; Spies, Maria; Antony, Edwin; and Zhang, Xiaodong, "A Structural and Dynamic Model for the Assembly of Replication Protein A on Single-Stranded DNA" (2018). Biological Sciences Faculty Research and Publications. 669.
https://epublications.marquette.edu/bio_fac/669
Comments
Published version. Nature Communications, Vol. 9, Article number: 5447 (2018). DOI. © 2018 Springer Nature Publishing AG. Used with permission.
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