|
PLANT PHYSIOLOGY , Vol 111, Issue 2 533-540, Copyright © 1996 by American Society of Plant Biologists
|
WHOLE PLANT, ENVIRONMENTAL, AND STRESS PHYSIOLOGY |
Iron and Copper Nutrition-Dependent Changes in Protein Expression in a Tomato Wild Type and the Nicotianamine-Free Mutant chloronerva
A. Herbik, A. Giritch, C. Horstmann, R. Becker, H. J. Balzer, H. Baumlein and U. W. Stephan
Institut fur Pflanzengenetik und Kulturpflanzenforschung, Corrensstrasse 3, D-06466 Gatersleben, Germany
The nicotianamine-deficient mutant chloronerva resembles phenotypically an
Fe-deficient plant despite the high accumulation of Fe in the leaves,
whereas it suffers from Cu deficiency in the shoot. Two-dimensional
electrophoretic separation of proteins from root tips and leaves of
wild-type Lycopersicon esculentum Mill. cv Bonner Beste and the mutant
grown with and without Fe showed a number of consistent differences. In
root tips of the Fe-deficient wild type and the Fe-sufficient as well as
the Fe-deficient mutant, the expression of glyceraldehyde-3-phosphate
dehydrogenase, formate dehydrogenase, and ascorbate peroxidase was
increased. In leaves of the Fe-sufficient and -deficient mutant,
Cu-containing chloroplastic and cytosolic superoxide dismutase (Cu-Zn) and
plastocyanin (Cu) were nearly absent. This low plastocyanin content could
be restored by supplying Cu via the xylem, but the superoxide dismutase
levels could not be increased by this treatment. The differences in the
protein patterns between wild type and mutant indicate that the apparent Fe
deficiency of mutant plants led to an increase in enzymes involved in
anaerobic metabolism as well as enzymes involved in stress defense. The
biosynthesis of plastocyanin was diminished in mutant leaves, but it was
differentially induced by increased Cu content.
This article has been cited by other articles:
|
|
|
|
 
C. Curie, G. Cassin, D. Couch, F. Divol, K. Higuchi, M. Le Jean, J. Misson, A. Schikora, P. Czernic, and S. Mari
Metal movement within the plant: contribution of nicotianamine and yellow stripe 1-like transporters
Ann. Bot.,
January 1, 2009;
103(1):
1 - 11.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. Irtelli, W. A. Petrucci, and F. Navari-Izzo
Nicotianamine and histidine/proline are, respectively, the most important copper chelators in xylem sap of Brassica carinata under conditions of copper deficiency and excess
J. Exp. Bot.,
January 1, 2009;
60(1):
269 - 277.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. S. Green and E. E. Rogers
FRD3 Controls Iron Localization in Arabidopsis
Plant Physiology,
September 1, 2004;
136(1):
2523 - 2531.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. Fourcroy, G. Vansuyt, S. Kushnir, D. Inze, and J.-F. Briat
Iron-Regulated Expression of a Cytosolic Ascorbate Peroxidase Encoded by the APX1 Gene in Arabidopsis Seedlings
Plant Physiology,
February 1, 2004;
134(2):
605 - 613.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. Uhde-Stone, K. E. Zinn, M. Ramirez-Yanez, A. Li, C. P. Vance, and D. L. Allan
Nylon Filter Arrays Reveal Differential Gene Expression in Proteoid Roots of White Lupin in Response to Phosphorus Deficiency
Plant Physiology,
March 1, 2003;
131(3):
1064 - 1079.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
O. Thimm, B. Essigmann, S. Kloska, T. Altmann, and T. J. Buckhout
Response of Arabidopsis to Iron Deficiency Stress as Revealed by Microarray Analysis
Plant Physiology,
November 1, 2001;
127(3):
1030 - 1043.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. F. López-Millán, F. Morales, S. Andaluz, Y. Gogorcena, A. Abadía, J. D. L. Rivas, and J. Abadía
Responses of Sugar Beet Roots to Iron Deficiency. Changes in Carbon Assimilation and Oxygen Use
Plant Physiology,
October 1, 2000;
124(2):
885 - 898.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
K. Suzuki, R. Itai, K. Suzuki, H. Nakanishi, N.-K. Nishizawa, E. Yoshimura, and S. Mori
Formate Dehydrogenase, an Enzyme of Anaerobic Metabolism, Is Induced by Iron Deficiency in Barley Roots
Plant Physiology,
February 1, 1998;
116(2):
725 - 732.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
