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@article{1798275,
author = {Špírek, Mário and Taylor, M. R. G. and Beláň, Ondrej and Boulton, S. J. and Krejčí, Lumír},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41467-021-25830-x},
keywords = {RAD51; nucleotide proofreading functions},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function},
url = {https://www.nature.com/articles/s41467-021-25830-x},
volume = {12},
year = {2021}
}
TY - JOUR
ID - 1798275
AU - Špírek, Mário - Taylor, M. R. G. - Beláň, Ondrej - Boulton, S. J. - Krejčí, Lumír
PY - 2021
TI - Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function
JF - Nature Communications
VL - 12
IS - 1
SP - 1-12
EP - 1-12
PB - Nature Publishing Group
SN - 20411723
KW - RAD51
KW - nucleotide proofreading functions
UR - https://www.nature.com/articles/s41467-021-25830-x
N2 - The RAD51 recombinase assembles as helical nucleoprotein filaments on single-stranded DNA (ssDNA) and mediates invasion and strand exchange with homologous duplex DNA (dsDNA) during homologous recombination (HR), as well as protection and restart of stalled replication forks. Strand invasion by RAD51-ssDNA complexes depends on ATP binding. However, RAD51 can bind ssDNA in non-productive ADP-bound or nucleotide-free states, and ATP-RAD51-ssDNA complexes hydrolyse ATP over time. Here, we define unappreciated mechanisms by which the RAD51 paralog complex RFS-1/RIP-1 limits the accumulation of RAD-51-ssDNA complexes with unfavorable nucleotide content. We find RAD51 paralogs promote the turnover of ADP-bound RAD-51 from ssDNA, in striking contrast to their ability to stabilize productive ATP-bound RAD-51 nucleoprotein filaments. In addition, RFS-1/RIP-1 inhibits binding of nucleotide-free RAD-51 to ssDNA. We propose that 'nucleotide proofreading' activities of RAD51 paralogs co-operate to ensure the enrichment of active, ATP-bound RAD-51 filaments on ssDNA to promote HR. A RAD51 paralog complex, RFS-1/RIP-1, is shown to control ssDNA binding and dissociation by RAD-51 differentially in the presence and absence of nucleotide cofactors. These nucleotide proofreading activities drive a preferential accumulation of RAD-51-ssDNA complexes with optimal nucleotide content.
ER -
ŠPÍREK, Mário, M. R. G. TAYLOR, Ondrej BELÁŇ, S. J. BOULTON a Lumír KREJČÍ. Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~1-12. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-25830-x.
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