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Plant Physiol, February 2002, Vol. 128, pp. 578-590
FQR1, a Novel Primary Auxin-Response Gene, Encodes
a Flavin Mononucleotide-Binding Quinone Reductase1
Marta J.
Laskowski,*
Kate A.
Dreher,2
Mary A.
Gehring,3
Steffen
Abel,
Arminda L.
Gensler,4 and
Ian M.
Sussex
Department of Biology, Williams College, Williamstown,
Massachusetts 01267 (M.J.L., K.A.D., M.A.G.,
A.L.G.); Department of Vegetable Crops, University of
California, Davis, California 95616 (K.A.D., S.A.); and Department
of Molecular, Cellular, and Developmental Biology, Yale University, New
Haven, Connecticut 06520 (I.M.S.)
FQR1 is a novel primary auxin-response gene that
codes for a flavin mononucleotide-binding flavodoxin-like quinone
reductase. Accumulation of FQR1 mRNA begins within 10 min of indole-3-acetic acid application and reaches a maximum of
approximately 10-fold induction 30 min after treatment. This increase
in FQR1 mRNA abundance is not diminished by the protein
synthesis inhibitor cycloheximide, demonstrating that
FQR1 is a primary auxin-response gene. Sequence analysis
reveals that FQR1 belongs to a family of flavin mononucleotide-binding quinone reductases. Partially purified His-tagged FQR1 isolated from
Escherichia coli catalyzes the transfer of electrons
from NADH and NADPH to several substrates and exhibits in vitro quinone reductase activity. Overexpression of FQR1 in plants
leads to increased levels of FQR1 protein and quinone reductase
activity, indicating that FQR1 functions as a quinone reductase in
vivo. In mammalian systems, glutathione S-transferases
and quinone reductases are classified as phase II detoxification
enzymes. We hypothesize that the auxin-inducible glutathione
S-transferases and quinone reductases found in plants
also act as detoxification enzymes, possibly to protect against
auxin-induced oxidative stress.
1
This work was supported in part by the National
Science Foundation (grant no. IBN-920597/DIR-9104374). Support for
K.A.D. was provided by Williams College and a Molecular and Cellular Biology Training Grant Award, University of California-Davis. Support
for M.A.G. was provided by a Howard Hughes Medical Institute grant to
Williams College.
2
Present address: Plant Biology Graduate Group, Section
of Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616.
3
Present address: Department of Plant and Microbial
Biology, University of California, Berkeley, Berkeley, CA 94720.
4
Present address: 1445 Private Property Court Apt 18, Gloucester Point, VA 23062.
*
Corresponding author; e-mail mlaskowski{at}williams.edu; fax
413-597-3495.
© 2002 American Society of Plant Physiologists
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