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Journal ArticleDOI

Dynamic regulatory interactions of rad51, rad52, and replication protein-a in recombination intermediates.

Tomohiko Sugiyama, +1 more
- 03 Jul 2009 - 
- Vol. 390, Iss: 1, pp 45-55
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TLDR
These results suggest a regulatory role for Rad51 that suppresses ssDNA annealing and facilitates DNA strand invasion, where Rad51-double-stranded DNA may inhibit illegitimate second-end capture to ensure the error-free repair of a DNA double-strand break.
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This article is published in Journal of Molecular Biology.The article was published on 2009-07-03. It has received 49 citations till now. The article focuses on the topics: Replication protein A & Strand invasion.

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Citations
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Journal ArticleDOI

Concentration-Dependent Exchange of Replication Protein a on Single-Stranded DNA Revealed by Single-Molecule Imaging

TL;DR: The results reveal an unanticipated exchange between bound and free RPA suggesting a binding mechanism that can confer exceptionally slow off rates, yet also enables rapid displacement through a direct exchange mechanism that is reliant upon the presence of free ssDNA-binding proteins in solution.
Journal ArticleDOI

Replication protein A: directing traffic at the intersection of replication and repair.

TL;DR: This review summarizes the current understanding of RPA structure, phosphorylation and protein-protein interactions in mediating these DNA metabolic processes.
Journal ArticleDOI

Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes

TL;DR: In contrast to the wild type protein, hRad52RQK/AAA and hRad521–212 mutants with impaired ability to bind hR PA protein competed with hRPA for binding to ssDNA and failed to counteract hRpa-mediated duplex destabilization highlighting the importance of hRad 52-hRPA interactions in promoting efficient DNA annealing.
Journal ArticleDOI

DNA-PK, ATM and ATR collaboratively regulate p53-RPA interaction to facilitate homologous recombination DNA repair.

TL;DR: The results reveal a mechanism for the crosstalk between HR repair and NHEJ through the co-regulation of p53–RPA interaction by DNA-PK, ATM and ATR.
Journal ArticleDOI

Protein dynamics during presynaptic-complex assembly on individual single-stranded DNA molecules

TL;DR: This work illustrates the spatial and temporal progression of the association of RPA and Rad52 with the presynaptic complex and reveals a new RPA–Rad52–Rad51–ssDNA intermediate, with implications for how the activities of Rad52 and RPA are coordinated with Rad51 during the later stages of recombination.
References
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Book ChapterDOI

Escherichia coli phage T4 topoisomerase.

TL;DR: This chapter explains the interaction of T4 topoisomerase with DNA in the origin region of the T4 chromosome and attempts to reconstitute the initiation reaction in vitro in order to test this and other models for the involvement of the enzyme in the DNA replication process.
Journal ArticleDOI

In vivo assembly and disassembly of Rad51 and Rad52 complexes during double-strand break repair

TL;DR: Evidence is presented for three distinct roles for Rad52 in recombination: a presynaptic role necessary for Rad51 assembly, a synaptic role with Rad51 filaments, and a postsynaptic role after Rad51 dissociates.
Journal ArticleDOI

Rfc4 Interacts with Rpa1 and Is Required for Both DNA Replication and DNA Damage Checkpoints in Saccharomyces cerevisiae

TL;DR: In addition to its essential role as part of the clamp loader in DNA replication, RFC4 plays a role as a sensor in multiple DNA checkpoint pathways, suggesting that a physical interaction between Rfc4 and Rpa1N is required for both roles.
Journal ArticleDOI

DNA Repair Synthesis Facilitates RAD52-Mediated Second-End Capture during DSB Repair

TL;DR: It is shown that DNA repair synthesis, catalyzed by human DNA polymerase eta (poleta) acting upon the priming strand of a D loop, leads to capture and annealing of the second end of a resected DSB in reactions mediated by RAD52 protein.
Journal ArticleDOI

Visualisation of human rad52 protein and its complexes with hrad51 and DNA

TL;DR: In this article, the first direct visualisation of protein-DNA complexes formed by the human Rad51 and Rad52 recombination/repair proteins was presented, where the Rad52 protein self-associates to form ring structures with a diameter of approximately 10 nm, each ring contains a hole at its centre.
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