|
PLANT PHYSIOLOGY , Vol 113, Issue 4 1329-1341, Copyright © 1997 by American Society of Plant Biologists
|
GENE REGULATION AND MOLECULAR GENETICS |
Characterization and Expression of NAD(H)-Dependent Glutamate Dehydrogenase Genes in Arabidopsis
F. J. Turano, S. S. Thakkar, T. Fang and J. M. Weisemann
United States Department of Agriculture, Agricultural Research Service, Climate Stress Laboratory, Beltsville, Maryland 20705 (F.J.T., S.S.T., T.F.)
Two distinct cDNA clones encoding NAD(H)-dependent glutamate dehydrogenase
(NAD[H]-GDH) in Arabidopsis thaliana were identified and sequenced. The
genes corresponding to these cDNA clones were designated GDH1 and GDH2.
Analysis of the deduced amino acid sequences suggest that both gene
products contain putative mitochondrial transit polypeptides and NAD(H)-
and [alpha]-ketoglutarate-binding domains. Subcellular fractionation
confirmed the mitochondrial location of the NAD(H)-GDH isoenzymes. In
addition, a putative EF-hand loop, shown to be associated with Ca2+
binding, was identified in the GDH2 gene product but not in the GDH1 gene
product. GDH1 encodes a 43.0-kD polypeptide, designated [alpha], and GDH2
encodes a 42.5-kD polypeptide, designated [beta]. The two subunits combine
in different ratios to form seven NAD(H)-GDH isoenzymes. The
slowest-migrating isoenzyme in a native gel, GDH1, is a homohexamer
composed of [alpha] subunits, and the fastest-migrating isoenzyme, GDH7, is
a homohexamer composed of [beta] subunits. GDH isoenzymes 2 through 6 are
heterohexamers composed of different ratios of [alpha] and [beta] subunits.
NAD(H)-GDH isoenzyme patterns varied among different plant organs and in
leaves of plants irrigated with different nitrogen sources or subjected to
darkness for 4 d. Conversely, there were little or no measurable changes in
isoenzyme patterns in roots of plants treated with different nitrogen
sources. In most instances, changes in isoenzyme patterns were correlated
with relative differences in the level of [alpha] and [beta] subunits.
Likewise, the relative difference in the level of [alpha] or [beta]
subunits was correlated with changes in the level of GDH1 or GDH2
transcript detected in each sample, suggesting that NAD(H)-GDH activity is
controlled at least in part at the transcriptional level.
This article has been cited by other articles:
|
|
|
|
 
K. G. Zulak, M. F. Khan, J. Alcantara, D. C. Schriemer, and P. J. Facchini
Plant Defense Responses in Opium Poppy Cell Cultures Revealed by Liquid Chromatography-Tandem Mass Spectrometry Proteomics
Mol. Cell. Proteomics,
January 1, 2009;
8(1):
86 - 98.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. G. Forde and P. J. Lea
Glutamate in plants: metabolism, regulation, and signalling
J. Exp. Bot.,
July 1, 2007;
58(9):
2339 - 2358.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. P. Purnell and J. R. Botella
Tobacco Isoenzyme 1 of NAD(H)-Dependent Glutamate Dehydrogenase Catabolizes Glutamate in Vivo
Plant Physiology,
January 1, 2007;
143(1):
530 - 539.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. S. Skopelitis, N. V. Paranychianakis, K. A. Paschalidis, E. D. Pliakonis, I. D. Delis, D. I. Yakoumakis, A. Kouvarakis, A. K. Papadakis, E. G. Stephanou, and K. A. Roubelakis-Angelakis
Abiotic Stress Generates ROS That Signal Expression of Anionic Glutamate Dehydrogenases to Form Glutamate for Proline Synthesis in Tobacco and Grapevine
PLANT CELL,
October 1, 2006;
18(10):
2767 - 2781.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J.-X. Fontaine, F. Saladino, C. Agrimonti, M. Bedu, T. Terce-Laforgue, T. Tetu, B. Hirel, F. M. Restivo, and F. Dubois
Control of the Synthesis and Subcellular Targeting of the Two GDH Genes Products in Leaves and Stems of Nicotiana plumbaginifolia and Arabidopsis thaliana
Plant Cell Physiol.,
March 1, 2006;
47(3):
410 - 418.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Terce-Laforgue, F. Dubois, S. Ferrario-Mery, M.-A. Pou de Crecenzo, R. Sangwan, and B. Hirel
Glutamate Dehydrogenase of Tobacco Is Mainly Induced in the Cytosol of Phloem Companion Cells When Ammonia Is Provided Either Externally or Released during Photorespiration
Plant Physiology,
December 1, 2004;
136(4):
4308 - 4317.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Kang and F. J. Turano
The putative glutamate receptor 1.1 (AtGLR1.1) functions as a regulator of carbon and nitrogen metabolism in Arabidopsis thaliana
PNAS,
May 27, 2003;
100(11):
6872 - 6877.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
V. Kruft, H. Eubel, L. Jansch, W. Werhahn, and H.-P. Braun
Proteomic Approach to Identify Novel Mitochondrial Proteins in Arabidopsis
Plant Physiology,
December 1, 2001;
127(4):
1694 - 1710.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. M.A. Dirk, M. A. Williams, and R. L. Houtz
Eukaryotic Peptide Deformylases. Nuclear-Encoded and Chloroplast-Targeted Enzymes in Arabidopsis
Plant Physiology,
September 1, 2001;
127(1):
97 - 107.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Aubert, R. Bligny, R. Douce, E. Gout, R.G. Ratcliffe, and J.K.M. Roberts
Contribution of glutamate dehydrogenase to mitochondrial glutamate metabolism studied by 13C and 31P nuclear magnetic resonance
J. Exp. Bot.,
January 1, 2001;
52(354):
37 - 45.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. L. Smith and K. C. Gross
A Family of at Least Seven beta -Galactosidase Genes Is Expressed during Tomato Fruit Development
Plant Physiology,
July 1, 2000;
123(3):
1173 - 1184.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
F. J. Turano and T. K. Fang
Characterization of Two Glutamate Decarboxylase cDNA Clones from Arabidopsis
Plant Physiology,
August 1, 1998;
117(4):
1411 - 1421.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
D. L. Smith, D. A. Starrett, and K. C. Gross
A Gene Coding for Tomato Fruit beta -Galactosidase II Is Expressed during Fruit Ripening . Cloning, Characterization, and Expression Pattern
Plant Physiology,
June 1, 1998;
117(2):
417 - 423.
[Abstract]
[Full Text]
|
|
|
|
|
