Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (34)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Casati, P.
Right arrow Articles by Andreo, C. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Casati, P.
Right arrow Articles by Andreo, C. S.
Agricola
Right arrow Articles by Casati, P.
Right arrow Articles by Andreo, C. S.

Plant Physiol, August 2000, Vol. 123, pp. 1611-1622

Induction of a C4-Like Mechanism of CO2 Fixation in Egeria densa, a Submersed Aquatic Species1

Paula Casati,2 María V. Lara,2 and Carlos S. Andreo*

Centro de Estudios Fotosintéticos y Bioquímicos, Universidad Nacional de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas, Suipacha 531, 2000 Rosario, Argentina

The expression of phosphoenolpyruvate carboxylase (PEPC) and NADP-malic enzyme (NADP-ME) in Egeria densa leaves was studied under low temperature and light (LTL) following incubation under high temperature and light (HTL), conditions previously shown to induce high and low CO2 compensation points, respectively. Transfer from LTL to HTL conditions induced increases in the activities and amounts of both enzymes. One NADP-ME isoform was observed in induced and uninduced samples. Two isoforms of PEPC were expressed, with the lower Mr isoform being induced by HTL. NADP-ME showed properties similar to those of the isoform in C3 species. The inducible PEPC isoform has a low Km for both substrates. PEPC kinetic and regulatory properties (Vmax and Km for phosphoenolpyruvate, and I50 for L-malate) are different in samples taken in the dark from those in the light, indicating that some modification of PEPC may be occurring during the day. Finally, abscisic acid induced the expression of PEPC and NADP-ME in a manner similar to temperature induction, except that the activities of both PEPC isoforms were increased. A different signaling system may exist in this species in response to high temperature or abscisic acid, both of which induce changes in photosynthetic metabolism.


1 This work was funded by grants from the Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and from the Agencia Nacional de Promoción Científica y Tecnológica (BID 802/0C-AR PICT no. 1-03397). P.C. and M.V.L. are fellows from CONICET and C.S.A. is a Researcher Career Member of the same institution.

2 These authors contributed equally to this work.

* Corresponding author; e-mail candreo{at}agatha.unr.edu.ar; fax 54-341-4370044.

© 2000 American Society of Plant Physiologists



This article has been cited by other articles:


Home page
Plant Cell PhysiolHome page
G. L. Muller, M. F. Drincovich, C. S. Andreo, and M. V. Lara
Nicotiana tabacum NADP-Malic Enzyme: Cloning, Characterization and Analysis of Biological Role
Plant Cell Physiol., March 1, 2008; 49(3): 469 - 480.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
S. Rao, J. Reiskind, and G. Bowes
Light Regulation of the Photosynthetic Phosphoenolpyruvate Carboxylase (PEPC) in Hydrilla verticillata
Plant Cell Physiol., September 1, 2006; 47(9): 1206 - 1216.
[Abstract] [Full Text] [PDF]


Home page
ANN BOT (LOND)Home page
L. MOMMER and E. J. W. VISSER
Underwater Photosynthesis in Flooded Terrestrial Plants: A Matter of Leaf Plasticity
Ann. Bot., September 1, 2005; 96(4): 581 - 589.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
M. V. Lara, M. F. Drincovich, G. L. Muller, V. G. Maurino, and C. S. Andreo
NADP-malic Enzyme and Hsp70: Co-purification of Both Proteins and Modification of NADP-malic Enzyme Properties by Association with Hsp70
Plant Cell Physiol., June 1, 2005; 46(6): 997 - 1006.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
B. Chinthapalli, J. Murmu, and A. S. Raghavendra
Dramatic difference in the responses of phosphoenolpyruvate carboxylase to temperature in leaves of C3 and C4 plants
J. Exp. Bot., February 1, 2003; 54(383): 707 - 714.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
S. K. Rao, N. C. Magnin, J. B. Reiskind, and G. Bowes
Photosynthetic and Other Phosphoenolpyruvate Carboxylase Isoforms in the Single-Cell, Facultative C4 System of Hydrilla verticillata
Plant Physiology, October 1, 2002; 130(2): 876 - 886.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
R. C. Leegood
C4 photosynthesis: principles of CO2 concentration and prospects for its introduction into C3 plants
J. Exp. Bot., April 1, 2002; 53(369): 581 - 590.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
R. E. Hausler, H.-J. Hirsch, F. Kreuzaler, and C. Peterhansel
Overexpression of C4-cycle enzymes in transgenic C3 plants: a biotechnological approach to improve C3-photosynthesis
J. Exp. Bot., April 1, 2002; 53(369): 591 - 607.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
O. Ueno
Environmental Regulation of C3 and C4 Differentiation in the Amphibious Sedge Eleocharis vivipara
Plant Physiology, December 1, 2001; 127(4): 1524 - 1532.
[Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
M. V. Lara, P. Casati, and C. S. Andreo
In vivo Phosphorylation of Phosphoenolpyruvate Carboxylase in Egeria densa, a Submersed Aquatic Species
Plant Cell Physiol., April 1, 2001; 42(4): 441 - 445.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2000 by the American Society of Plant Biologists