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ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination
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ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination
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Journal Article
ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination
2017
Overview
Homologous recombination (HR), catalyzed in an evolutionarily conserved manner by active RecA/Rad51 nucleofilaments, maintains genomic integrity and promotes biological evolution and diversity. The structures of RecA/Rad51 nucleofilaments provide information critical for the entire HR process. By exploiting a unique capillary electrophoresis-laser-induced fluorescence polarization assay, we have discovered an active form of RecA nucleofilament, stimulated by ATP hydrolysis, that contains mainly unbound nucleotide sites. This finding was confirmed by a nuclease protection assay and electron microscopy (EM) imaging. We further found that these RecA-unsaturated filaments promote strand exchange
in vitro
and HR
in vivo
. RecA mutants (P67D and P67E), which only form RecA-unsaturated nucleofilaments, were able to mediate HR
in vitro
and
in vivo
, but mutants favoring the formation of the saturated nucleofilaments failed to support HR. We thus present a new model for RecA-mediated HR in which RecA utilizes its intrinsic DNA binding-dependent ATPase activity to remodel the nucleofilaments to a less saturated form and thereby promote HR.
Publisher
Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
