Kinetics and functional diversity among the five members of the NADP-malic enzyme family from Zea mays, a C4 species View Full Text


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Article Info

DATE

2013-05-07

AUTHORS

Clarisa E. Alvarez, Mariana Saigo, Ezequiel Margarit, Carlos S. Andreo, María F. Drincovich

ABSTRACT

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. More... »

PAGES

65-80

References to SciGraph publications

  • 1999-08. Malate metabolism by NADP-malic enzyme in plant defense in PHOTOSYNTHESIS RESEARCH
  • 1989-08. Two tobacco DNA-binding proteins with homology to the nuclear factor CREB in NATURE
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  • 2001-03. Non-photosynthetic `malic enzyme' from maize: a constituvely expressed enzyme that responds to plant defence inducers in PLANT MOLECULAR BIOLOGY
  • 2003. The C4 pathway: an efficient CO2 pump in PHOTOSYNTHESIS RESEARCH
  • 2010-04-10. Coexpression landscape in ATTED-II: usage of gene list and gene network for various types of pathways in JOURNAL OF PLANT RESEARCH
  • 2012-12-16. Fumarate and cytosolic pH as modulators of the synthesis or consumption of C4 organic acids through NADP-malic enzyme in Arabidopsis thaliana in PLANT MOLECULAR BIOLOGY
  • 2010-10-31. The developmental dynamics of the maize leaf transcriptome in NATURE GENETICS
  • 2008-07-13. Maize cytosolic NADP-malic enzyme (ZmCytNADP-ME): a phylogenetically distant isoform specifically expressed in embryo and emerging roots in PLANT MOLECULAR BIOLOGY
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  • 1994-12. The C3 plant Flaveria pringlei contains a plastidic NADP-malic enzyme which is orthologous to the C4 isoform of the C4 plant F. trinervia in PLANT MOLECULAR BIOLOGY
  • 2008-02-21. Arabidopsis thaliana NADP-malic enzyme isoforms: high degree of identity but clearly distinct properties in PLANT MOLECULAR BIOLOGY
  • 2004-04. Applied bioinformatics for the identification of regulatory elements in NATURE REVIEWS GENETICS
  • 2007-02-09. qBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data in GENOME BIOLOGY
  • 2010-08-31. Chapter 14 C4 Decarboxylases: Different Solutions for the Same Biochemical Problem, the Provision of CO2 to Rubisco in the Bundle Sheath Cells in C4 PHOTOSYNTHESIS AND RELATED CO2 CONCENTRATING MECHANISMS
  • 1996-03. The transcriptional activatorOpaque-2 controls the expression of a cytosolic form of pyruvate orthophosphate dikinase-1 in maize endosperms in MOLECULAR GENETICS AND GENOMICS
  • 2004-05. Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity in PLANT MOLECULAR BIOLOGY
  • 1994-03. Nucleotide sequence of a rice cDNA similar to a maize NADP-dependent malic enzyme in PLANT MOLECULAR BIOLOGY
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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/23649167


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    43 schema:description 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.
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