Imperial College London
Alternate

Dr Luke A. Yates

Faculty of Medicine, Department of Infectious Disease

Research Associate
 
 
 
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Contact

 

luke.yates

 
 
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Location

 

245Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@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}
}
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RIS format (EndNote, RefMan)

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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