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Acetyl - CoA carboxylase - evolution and inhibition
Chalupská, Dominika ; Čeřovská, Noemi (advisor) ; Plchová, Helena (referee) ; Vlček, Čestmír (referee)
Abstract
Acetyl-CoA
carboxylase
(ACC)
is
a
key
enzyme
of
fatty
acid
metabolism
with
multiple
isozymes
often
expressed
in
different
eukaryotic
cellular
compartments.
In
agriculture,
inhibitors
of
plastid
ACC
are
used
as
efficient
herbicides
against
grass
weed.
However,
grass
weed
populations
resistant
to
aryloxyphenoxypropionate
(APP)
and
cyclohexanedione
(CHD)
herbicides
represent
a
major
problem
for
sustainable
agriculture.
Using
PCR
and
sequencing
it
was
found
out
that
five
amino
acid
substitutions
in
plastid
ACC
were
correlated
with
herbicide
resistance
of
Avena
sterilis
ssp.
ludoviciana
Durieu
populations
from
the
northern
grain-growing
region
of
Australia:
Trp-1,999-Cys,
Trp-2,027- Cys,
Ile-2,041-Asn,
Asp-2,078-Gly
and
Gly-2,096-Ala.
We
showed,
using
a
yeast
gene- replacement
system,
that
these
single-site
mutations
also
confer
herbicide
resistance
to
wheat
plastid
ACCase:
Asp-2,078-Gly
confers
resistance
to
APPs
and
CHDs,
Trp-2,027-Cys
and
Ile-2,041-Asn
confer
resistance
to
APPs,
and
Trp-1,999-Cys
confers
resistance
only
to
fenoxaprop.
These
mutations
are
very
likely
to
confer
resistance
to
any
grass
weed
species
under
selection
imposed
by
the
extensive
agricultural
use
of
the
herbicides.
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