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Artículo

Functional and kinetic diversity among the five members of the NADP-malic enzyme family from Zea mays, a C4 species

Alvarez, Clarisa EsterIcon ; Saigo, MarianaIcon ; Margarit, EzequielIcon ; Andreo, Carlos SantiagoIcon ; Drincovich, Maria FabianaIcon
Fecha de publicación: 04/2013
Editorial: Springer
Revista: Photosynthesis Research
ISSN: 0166-8595
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Bioquímica y Biología Molecular

Resumen

NADP-malic enzyme (NADP-ME) is involved in different metabolic pathways in several organisms due to the relevant physiological functions of the substrates and products of its reaction. In plants, it is one of the most important proteins that were recruited to fulfil key roles in C4 photosynthesis. Recent advances in genomics allowed the characterization of the complete set of NADP-ME genes from some C3 species, as Arabidopsis thaliana and Oryza sativa; however, the characterization of the complete NADP-ME family from a C4 species has not been performed yet. In this study, while taking advantage of the complete Zea mays genome sequence recently released, the characterization of the whole NADP-ME family is presented. The maize NADP-ME family is composed of five genes, two encoding plastidic NADP-MEs (ZmC4- and ZmnonC4-NADP-ME), and three cytosolic enzymes (Zmcyt1-, Zmcyt2-, and Zmcyt3-NADP-ME). The results presented clearly show that each maize NADP-ME displays particular organ distribution, response to stress stimuli, and differential biochemical properties. Phylogenetic footprinting studies performed with the NADP-MEs from several grasses, indicate that four members of the maize NADP-ME family share conserved transcription factor binding motifs with their orthologs, indicating conserved physiological functions for these genes in monocots. Based on the results obtained in this study, and considering the biochemical plasticity shown by the NADP-ME, it is discussed the relevance of the presence of a multigene family, in which each member encodes an isoform with particular biochemical properties, in the evolution of the C4 NADP-ME, improved to fulfil the requirements for an efficient C4 mechanism.
Palabras clave: Zea Mays , Metabolismo C4 , Evolucion , Enzima Malica
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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
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URI: http://hdl.handle.net/11336/7827
URL: http://link.springer.com/article/10.1007%2Fs11120-013-9839-9
DOI: http://dx.doi.org/10.1007/s11120-013-9839-9
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Articulos(CEFOBI)
Articulos de CENTRO DE EST.FOTOSINTETICOS Y BIOQUIMICOS (I)
Citación
Alvarez, Clarisa Ester; Saigo, Mariana; Margarit, Ezequiel; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Functional and kinetic diversity among the five members of the NADP-malic enzyme family from Zea mays, a C4 species; Springer; Photosynthesis Research; 115; 1; 4-2013; 65-80
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