Plastidial NADP-malic enzymes from grasses: Unraveling the way to the C4 specific isoforms

被引:16
|
作者
Saigo, Mariana [1 ]
Alvarez, Clarisa E. [1 ]
Andreo, Carlos S. [1 ]
Drincovich, Maria F. [1 ]
机构
[1] Univ Nacl Rosario, Ctr Estudios Fotosintet & Bioquim CEFOBI, RA-2000 Rosario, Santa Fe, Argentina
关键词
C-4; photosynthesis; NADP-malic enzyme; Maize; Sorghum; Rice; Structure-function relationship; MAIZE C(4)NADP-MALIC ENZYME; RELATIVE QUANTIFICATION; CRYSTAL-STRUCTURE; MALATE; EVOLUTION; ARABIDOPSIS; SOFTWARE; PROTEINS; SORGHUM; GENOME;
D O I
10.1016/j.plaphy.2012.11.009
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Malic enzyme is present in many plant cell compartments such as plastids, cytosol and mitochondria. Particularly relevant is the plastidial isoform that participates in the C-4 cycle providing CO2 to RuBisCO in C-4 species. This type of photosynthesis is more frequent among grasses where anatomical pre-conditioning would have facilitated the evolution of the C-4 syndrome. In maize (C-4 grass), the photosynthetic NADP dependent Malic enzyme (ZmC(4)-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) and the closest related non-photosynthetic isoform (ZmnonC(4)-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) are both plastidial but differ in expression pattern, kinetics and structure. Features like high catalytic efficiency, inhibition by high malate concentration at pH 7.0, redox modulation and tetramerization are characteristic of the photosynthetic NADP-ME. In this work, the proteins encoded by sorghum (C-4 grass) and rice (C-3 grass) NADP-ME genes, orthologues of the plastidial NADP-MEs from maize, were recombinantly expressed, purified and characterized. In a global comparison, we could identify a small group of residues which may explain the special features of C-4 enzymes. Overall, the present work presents biochemical and molecular data that helps to elucidate the changes that took place in the evolution of C-4 NADP-ME in grasses. (c) 2012 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:39 / 48
页数:10
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