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hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity

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NuclAcidsRes2011_Richard_3643_51.pdf (3.915Mb)
Date
05/2011
Author
Richard, Derek J.
Cubeddu, Liza
Urquhart, Aaron J.
Bain, Amanda
Bolderson, Emma
Menon, Dinoop
White, Malcolm F.
Khanna, Kum Kum
Keywords
Replication protein-a
Binding-protein
Homologous recombination
MRE11-RAD50-NBS1 COMPLEX
Genomic stability
S-phase
ATM
Activation
MRE11
Checkpoint
QH426 Genetics
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Abstract
hSSB1 is a recently discovered single-stranded DNA binding protein that is essential for efficient repair of DNA double-strand breaks (DSBs) by the homologous recombination pathway. hSSB1 is required for the efficient recruitment of the MRN complex to sites of DSBs and for the efficient initiation of ATM dependent signalling. Here we explore the interplay between hSSB1 and MRN. We demonstrate that hSSB1 binds directly to NBS1, a component of the MRN complex, in a DNA damage independent manner. Consistent with the direct interaction, we observe that hSSB1 greatly stimulates the endo-nuclease activity of the MRN complex, a process that requires the C-terminal tail of hSSB1. Interestingly, analysis of two point mutations in NBS1, associated with Nijmegen breakage syndrome, revealed weaker binding to hSSB1, suggesting a possible disease mechanism.
Citation
Richard , D J , Cubeddu , L , Urquhart , A J , Bain , A , Bolderson , E , Menon , D , White , M F & Khanna , K K 2011 , ' hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity ' , Nucleic Acids Research , vol. 39 , no. 9 , pp. 3643-3651 . https://doi.org/10.1093/nar/gkq1340
Publication
Nucleic Acids Research
Status
Peer reviewed
DOI
https://doi.org/10.1093/nar/gkq1340
ISSN
0305-1048
Type
Journal article
Rights
© The Author(s) 2011. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/3439

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