A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA

Luke A. Yates, Ricardo J. Aramayo, Nilisha Pokhrel, Colleen C. Caldwell, Joshua A. Kaplan, Rajika L. Perera, Maria Spies, Edwin Antony and Xiaodong Zhang ()
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Luke A. Yates: Imperial College London
Ricardo J. Aramayo: Imperial College London
Nilisha Pokhrel: Marquette University
Colleen C. Caldwell: University of Iowa
Joshua A. Kaplan: Imperial College London
Rajika L. Perera: Imperial College London
Maria Spies: University of Iowa
Edwin Antony: Marquette University
Xiaodong Zhang: Imperial College London

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07883-7

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