10.5061/DRYAD.ZPC866T78
Ezraty, Benjamin
0000-0003-3818-6907
Aix-Marseille University
Henry, Camille
University of Wisconsin-Madison
Barras, Frederic
Institut Pasteur
Loiseau, Laurent
Aix-Marseille University
Vergnes, Alexandra
Aix-Marseille University
Vertommen, Didier
Université Catholique de Louvain
Mérida-Floriano, Angela
University of Seville
Chitteni-Pattu, Sindhu
University of Wisconsin–Madison
Wood, Elizabeth Anne
University of Wisconsin–Madison
Casadesús, Josep
University of Seville
Cox, Michael M.
University of Wisconsin–Madison
Redox controls RecA protein activity via reversible oxidation of its
methionine residues
Dryad
dataset
2020
2021-02-25T00:00:00Z
2021-02-25T00:00:00Z
en
7621340 bytes
6
CC0 1.0 Universal (CC0 1.0) Public Domain Dedication
Reactive oxygen species (ROS) cause damage to DNA and proteins. The RecA
protein plays a central role in the bacterial response to DNA damage. Here
we report that RecA itself is also targeted by ROS. In vivo consequences
of RecA oxidation include defects in SOS induction, DNA repair efficiency,
and P1 transduction. In vitro, oxidized RecA fails to display ATPase
activity, DNA strand exchange capacity and formation of nucleofilaments.
Consistently, mass spectrometry analysis of oxidized RecA revealed that
four out of 9 Met residues have been converted to methionine sulfoxide
(Met-O). Specifically, mimicking the oxidation of Met35 by changing it for
Gln caused complete loss of function whereas mimicking oxidation of Met164
resulted in constitutive SOS activation and loss of recombination
activity. The harmful effects of oxidation of RecA were mitigated by
repairing activities of methionine sulfoxide reductases MsrA and MsrB,
which suppressed all ROS-induced modifications of RecA activity. This work
identifies RecA as a substrate of the anti-ROS activity of the MsrA/B
enzymes. These findings indicate that under oxidative stress, MsrA/B
maintains a level of reduced functional RecA necessary to carry out both
efficient recombination and SOS regulation. The implication of this work
is that ROS might inflict damages to DNA both directly and indirectly via
hampering RecA repair activity.