2018
DOI: 10.1093/nar/gky111
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Human RAD51 rapidly forms intrinsically dynamic nucleoprotein filaments modulated by nucleotide binding state

Abstract: Formation of RAD51 filaments on single-stranded DNA is an essential event during homologous recombination, which is required for homology search, strand exchange and protection of replication forks. Formation of nucleoprotein filaments (NF) is required for development and genomic stability, and its failure is associated with developmental abnormalities and tumorigenesis. Here we describe the structure of the human RAD51 NFs and of its Walker box mutants using electron microscopy. Wild-type RAD51 filaments adop… Show more

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Cited by 42 publications
(44 citation statements)
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“…Similar to the results from a restriction-digest based assay (Wright & Heyer, 2014), there was an enrichment of D-loops near the 3′-end of ssDNA, while the 5′-end of homology had the lowest D-loop presence. This observation supports the model that Rad51 filament grows preferentially in a 5′-to-3′ direction (Qiu et al, 2013;Spirek et al, 2018), making it more likely for the D-loops to assemble at the 3′end of homology than at the 5′-end. Only D-loops in which the 3′-OH end is incorporated into the hDNA are competent for D-loop extension (Li & Heyer, 2009).…”
Section: Position Of D-loops Formed By a Supercoiled Donor Is Restricsupporting
confidence: 85%
“…Similar to the results from a restriction-digest based assay (Wright & Heyer, 2014), there was an enrichment of D-loops near the 3′-end of ssDNA, while the 5′-end of homology had the lowest D-loop presence. This observation supports the model that Rad51 filament grows preferentially in a 5′-to-3′ direction (Qiu et al, 2013;Spirek et al, 2018), making it more likely for the D-loops to assemble at the 3′end of homology than at the 5′-end. Only D-loops in which the 3′-OH end is incorporated into the hDNA are competent for D-loop extension (Li & Heyer, 2009).…”
Section: Position Of D-loops Formed By a Supercoiled Donor Is Restricsupporting
confidence: 85%
“…Although there were other differences in the proteins from these two studies, it is possible that the N-terminus constrains the filaments to a single conformation at the ATPase interface 8, 10 . More recently, high-resolution structural models of human RAD51 filaments have been obtained from cryo–electron microscopy reconstructions 11, 12 . Here, filaments formed with human RAD51 had only one conformation at the nucleotide-binding site.…”
Section: Rad51 Nucleoprotein Filaments: Variety In Form and Functionmentioning
confidence: 99%
“…Specifically, active filaments formed with ATP or an analog bound at the interface have a longer helical pitch and an “open” conformation 12, 15 . Recently, RAD51 nucleoprotein filaments with distinct mechanical properties have been defined for the wild-type protein (for example, persistence length, helical pitch, and rise per monomer) by a combination of single-molecule force spectroscopy and crystallography 13 .…”
Section: Rad51 Nucleoprotein Filaments: Variety In Form and Functionmentioning
confidence: 99%
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