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A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA
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A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA
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Journal Article
A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA
2018
Overview
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.
Replication Protein A (RPA) coats single stranded DNA (ssDNA) generated during DNA recombination, replication and repair. Here the authors present a structural model suggesting how RPA’s DNA-binding domains promote cooperative assembly of multiple RPAs on long ssDNA.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/125
/ 631/45
/ 631/535
/ 631/57
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Assembly
/ DNA
/ DNA, Single-Stranded - metabolism
/ Domains
/ Fluorescence Resonance Energy Transfer
/ Humanities and Social Sciences
/ Nuclease
/ Proteins
/ Replication Protein A - genetics
/ Replication Protein A - metabolism
/ Science
