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Plant Physiol, October 2000, Vol. 124, pp. 725-732
Rac-Related GTP-Binding Protein in Elicitor-Induced Reactive
Oxygen Generation by Suspension-Cultured Soybean
Cells1
Jumok
Park,
Hyun-Jung
Choi,
Sumin
Lee,
Taehoon
Lee,
Zhenbiao
Yang, and
Youngsook
Lee*
Division of Molecular Life Science, Pohang University of Science
and Technology, Pohang, 790-784, Korea (J.P., H.-J.C., S.L., T.L.,
Y.L.); and Department of Botany and Plant Sciences, University of
California, Riverside, California 92521-0124 (Z.Y.)
Plant cells produce reactive oxygen species (ROS) in response to
many stimuli. However, the mechanism of ROS biosynthesis remains
unclear. We have explored the hypothesis that the superoxide burst in
plants mechanistically resembles the oxidative burst in neutrophils.
First we have confirmed that ROS production, which occurs in
suspension-cultured soybean (Glycine max) cells in
response to hypo-osmotic shock, is inhibited by diphenylene iodonium,
an inhibitor of the flavin-dependent oxidase of neutrophils. Because a
Rac family G protein is an essential regulator of this NADPH oxidase,
and because many plant homologs of Rac have been cloned, we next
examined whether Rac-like proteins might be involved in the oxidative
burst in the soybean cells. We identified a Rac-like 21-kD soybean
protein that cross-reacts with antibodies to human Rac and garden pea
Rop and also binds [ -35S] GTP, a diagnostic trait of
small G proteins. This Rac-related protein translocated from the
cytosol to microsomes during the oxidative burst. Moreover, soybean
cells transiently transformed with either a dominant negative (RacN17)
or a dominant positive (RacV12) form of Rac1 showed the anticipated
altered responses to three different stimuli: hypo-osmotic shock,
oligo-GalUA, and harpin. In response to these stimuli, cells
transformed with RacN17 produced less ROS and cells transformed with
RacV12 generated more ROS than control cells. These results strongly
suggest that a Rac-related protein participates in the regulation of
ROS production in soybean cells, possibly via activation of an enzyme
complex similar to the NADPH oxidase of phagocytes in animal systems.
1
This work was supported by grants from the Korea
Science and Engineering Foundation (to Y.L.) and from the National
Science Foundation (no. MCD-9724047 to Z.Y.).
*
Corresponding author; e-mail ylee{at}postech.ac.kr; fax
82-54- 279-2199.
© 2000 American Society of Plant Physiologists
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