Plant Physiology 132:949-957 (2003)
© 2003 American Society of Plant Biologists
GENETICS AND MOLECULAR EVOLUTION
Identification and Expression Analysis of a Gene Encoding a Bacterial-Type Phosphoenolpyruvate Carboxylase from Arabidopsis and Rice1
Rosario Sánchez and
Francisco Javier Cejudo*
Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, Avda Américo Vespucio s/n, 41092-Sevilla, Spain
Phosphoenolpyruvate carboxylase (PEPC) is distributed in plants and bacteria but is not found in fungi and animal cells. Important motifs for enzyme activity and structure are conserved in plant and bacterial PEPCs, with the exception of a phosphorylation domain present at the N terminus of all plant PEPCs reported so far, which is absent in the bacterial enzymes. Here, we describe a gene from Arabidopsis, stated as Atppc4, encoding a PEPC, which shows more similarity to Escherichia coli than to plant PEPCs. Interestingly, this enzyme lacks the phosphorylation domain, hence indicating that it is a bacterial-type PEPC. Three additional PEPC genes are present in Arabidopsis, stated as Atppc1, Atppc2, and Atppc3, encoding typical plant-type enzymes. As most plant PEPC genes, Atppc1, Atppc2, and Atppc3 are formed by 10 exons interrupted by nine introns. In contrast, Atppc4 gene has an unusual structure formed by 20 exons. A bacterial-type PEPC gene was also identified in rice (Oryza sativa), stated as Osppc-b, therefore showing the presence of this type of PEPC in monocots. The phylogenetic analysis suggests that both plant-type and bacterial-type PEPCs diverged early during the evolution of plants from a common ancestor, probably the PEPC from  -proteobacteria. The diversity of plant-type PEPCs in C3, C4, and Crassulacean acid metabolism plants is indicative of the evolutionary success of the regulation by phosphorylation of this enzyme. Although at a low level, the bacterial-type PEPC genes are expressed in Arabidopsis and rice.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.102.019653.
1 This work was supported by the Ministerio de Ciencia y Tecnología (grant no. BMC2001–2366 and predoctoral fellowship to R.S.) and by Junta de Andalucía (Spain; grant no. CVI–182).
* Corresponding author; e-mail fjcejudo{at}us.es; fax 34–954460065.
Received December 23, 2002;
returned for revision January 26, 2003;
accepted January 30, 2003.
This article has been cited by other articles:
|
|
|
|
 
K. Kirchsteiger, P. Pulido, M. Gonzalez, and F. J. Cejudo
NADPH Thioredoxin Reductase C Controls the Redox Status of Chloroplast 2-Cys Peroxiredoxins in Arabidopsis thaliana
Mol Plant,
March 1, 2009;
2(2):
298 - 307.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A.-B. Feria, R. Alvarez, L. Cochereau, J. Vidal, S. Garcia-Maurino, and C. Echevarria
Regulation of Phosphoenolpyruvate Carboxylase Phosphorylation by Metabolites and Abscisic Acid during the Development and Germination of Barley Seeds
Plant Physiology,
October 1, 2008;
148(2):
761 - 774.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
F. Fauteux, F. Chain, F. Belzile, J. G. Menzies, and R. R. Belanger
The protective role of silicon in the Arabidopsis-powdery mildew pathosystem
PNAS,
November 14, 2006;
103(46):
17554 - 17559.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. V. Lara, S. D.X. Chuong, H. Akhani, C. S. Andreo, and G. E. Edwards
Species Having C4 Single-Cell-Type Photosynthesis in the Chenopodiaceae Family Evolved a Photosynthetic Phosphoenolpyruvate Carboxylase Like That of Kranz-Type C4 Species
Plant Physiology,
October 1, 2006;
142(2):
673 - 684.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. M. Perez-Ruiz, M. C. Spinola, K. Kirchsteiger, J. Moreno, M. Sahrawy, and F. J. Cejudo
Rice NTRC Is a High-Efficiency Redox System for Chloroplast Protection against Oxidative Damage
PLANT CELL,
September 1, 2006;
18(9):
2356 - 2368.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
V. Crowley, S. Gennidakis, and W. C. Plaxton
In vitro Proteolysis of Phosphoenolpyruvate Carboxylase from Developing Castor Oil Seeds by an Endogenous Thiol Endopeptidase
Plant Cell Physiol.,
November 1, 2005;
46(11):
1855 - 1862.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. E. Tripodi, W. L. Turner, S. Gennidakis, and W. C. Plaxton
In Vivo Regulatory Phosphorylation of Novel Phosphoenolpyruvate Carboxylase Isoforms in Endosperm of Developing Castor Oil Seeds
Plant Physiology,
October 1, 2005;
139(2):
969 - 978.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. Penaloza, G. Munoz, H. Salvo-Garrido, H. Silva, and L. J. Corcuera
Phosphate deficiency regulates phosphoenolpyruvate carboxylase expression in proteoid root clusters of white lupin
J. Exp. Bot.,
January 1, 2005;
56(409):
145 - 153.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. J. Serrato, J. M. Perez-Ruiz, M. C. Spinola, and F. J. Cejudo
A Novel NADPH Thioredoxin Reductase, Localized in the Chloroplast, Which Deficiency Causes Hypersensitivity to Abiotic Stress in Arabidopsis thaliana
J. Biol. Chem.,
October 15, 2004;
279(42):
43821 - 43827.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Sullivan, G. I. Jenkins, and H. G. Nimmo
Roots, Cycles and Leaves. Expression of the Phosphoenolpyruvate Carboxylase Kinase Gene Family in Soybean
Plant Physiology,
August 1, 2004;
135(4):
2078 - 2087.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. W. Shane, M. D. Cramer, S. Funayama-Noguchi, G. R. Cawthray, A. H. Millar, D. A. Day, and H. Lambers
Developmental Physiology of Cluster-Root Carboxylate Synthesis and Exudation in Harsh Hakea. Expression of Phosphoenolpyruvate Carboxylase and the Alternative Oxidase
Plant Physiology,
May 1, 2004;
135(1):
549 - 560.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
