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THE PLANT CELL, Vol 5, Issue 2 215-226, Copyright © 1993 by American Society of Plant Biologists
Molecular Characterization of NADH-Dependent Glutamate Synthase from Alfalfa Nodules
R. G. Gregerson, S. S. Miller, S. N. Twary, J. S. Gantt and C. P. Vance
U.S. Department of Agriculture-Agricultural Research Service, Plant Science Research Unit, St. Paul, Minnesota 55108
Alfalfa NADH-dependent glutamate synthase (NADH-GOGAT), together with
glutamine synthetase, plays a central role in the assimilation of
symbiotically fixed nitrogen into amino acids in root nodules. Antibodies
previously raised against purified NADH-GOGAT were employed to screen a
cDNA library prepared using RNA isolated from nodules of 20-day-old alfalfa
plants. A 7.2-kb cDNA clone was obtained that contained the entire protein
coding region of NADH-GOGAT. Analysis of this cDNA and determination of the
amino-terminal amino acids of the purified protein revealed that NADH-GOGAT
is synthesized as a 2194-amino acid protein that includes a 101-amino acid
presequence. The deduced amino acid sequence shares significant identity
with maize ferredoxin-dependent GOGAT, and with both large and small
subunits of Escherichia coli NADPH-GOGAT. DNA gel blot analysis of alfalfa
genomic DNA suggests the presence of a single NADH-GOGAT gene or a small
gene family. The expression of NADH-GOGAT mRNA, enzyme protein, and enzyme
activity was developmentally regulated in root nodules. A dramatic increase
in gene expression occurred coincidentally with the onset of nitrogen
fixation in the bacteroid, and was absent in both ineffective plants that
were nodulated with effective Rhizobium meliloti and effective plants that
had been nodulated with ineffective R. meliloti strains. Maximum NADH-GOGAT
expression, therefore, appears to require an effective, nitrogen-fixing
symbiosis.
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