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Quantitative Intercellular Localization of NADH-Dependent
Glutamate Synthase Protein in Different Types of Root Cells in Rice
Plants1
Toshihiko Hayakawa*,
Laura Hopkins,
Lucy J. Peat,
Tomoyuki Yamaya, and
Alyson K. Tobin
Laboratory of Plant Cell Biochemistry, Graduate School of
Agricultural Science, Tohoku University, 1-1
Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan (T.H.,
T.Y.); and Plant Science Laboratory, Sir Harold Mitchell Building,
School of Environmental and Evolutionary Biology, University of St.
Andrews, St. Andrews, United Kingdom KY16 9TH (L.H., L.J.P.,
A.K.T.)
The quantitative analysis with
immunogold-electron microscopy using a single-affinity-purified
anti-NADH-glutamate synthase (GOGAT) immunoglobulin G (IgG) as the
primary antibody showed that the NADH-GOGAT protein was present in
various forms of plastids in the cells of the epidermis and exodermis,
in the cortex parenchyma, and in the vascular parenchyma of root tips
(<10 mm) of rice (Oryza sativa) seedlings supplied with
1 mM NH4+ for 24 h. The values
of the mean immunolabeling density of plastids were almost equal among
these different cell types in the roots. However, the number of
plastids per individual cell type was not identical, and some parts of
the cells in the epidermis and exodermis contained large numbers of
plastids that were heavily immunolabeled. Although there was an
indication of labeling in the mitochondria using the
single-affinity-purified anti-NADH-GOGAT IgG, this was not confirmed
when a twice-affinity-purified IgG was used, indicating an exclusively
plastidial location of the NADH-GOGAT protein in rice roots. These
results, together with previous work from our laboratory (K. Ishiyama,
T. Hayakawa, and T. Yamaya [1998] Planta 204: 288-294), suggest that
the assimilation of exogeneously supplied NH4+
ions is primarily via the cytosolic glutamine synthetase/plastidial NADH-GOGAT cycle in specific regions of the epidermis and exodermis in
rice roots. We also discuss the role of the NADH-GOGAT protein in
vascular parenchyma cells.
1
This work was supported by a grant from the
Research for the Future Program of the Japanese Society for the
Promotion of Science (no. JSPS-RFTF96L00604); by Grants-in-Aid for
Scientific Research on Priority Areas (nos. 09274101 and 0927102), and
a Grant-in-Aid for Scientific Research (no. 08044187) from the Ministry
of Education, Science, Sports and Culture of Japan; by The Royal
Society (University Research Fellowship to A.K.T.); and by a grant from
the Biological and Biotechnological Sciences Research Council of the
United Kingdom (no. PO2582).
*
Corresponding author; e-mail toshi{at}biochem.tohoku.ac.jp; fax
81-22-717-8787.
Plant Physiol. (1999) 119: 409-416
Copyright Clearance Center: 0032-0889/99/119//08
© 1999 American Society of Plant Physiologists
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