In this section
@article{Yates:2018:10.1038/s41467-018-07883-7,
author = {Yates, LA and Aramayo, RJ and Pokhrel, N and Caldwell, CC and Kaplan, JA and Perera, RL and Spies, M and Anthony, E and Zhang, X},
doi = {10.1038/s41467-018-07883-7},
journal = {Nature Communications},
title = {A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA},
url = {http://dx.doi.org/10.1038/s41467-018-07883-7},
volume = {9},
year = {2018}
}
TY - JOUR
AB - 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.
AU - Yates,LA
AU - Aramayo,RJ
AU - Pokhrel,N
AU - Caldwell,CC
AU - Kaplan,JA
AU - Perera,RL
AU - Spies,M
AU - Anthony,E
AU - Zhang,X
DO - 10.1038/s41467-018-07883-7
PY - 2018///
SN - 2041-1723
TI - A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/s41467-018-07883-7
UR - http://hdl.handle.net/10044/1/66661
VL - 9
ER -
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