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Localization of arginine decarboxylase in tobacco plants
Author(s) -
Bortolotti Cristina,
Cordeiro Alexandra,
Alcázar Rubén,
Borrell Antoni,
CuliañezMacià Francisco A.,
Tiburcio Antonio F.,
Altabella Teresa
Publication year - 2004
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.0031-9317.2004.0216.x
Subject(s) - arginine decarboxylase , chloroplast , subcellular localization , nicotiana tabacum , biochemistry , complementary dna , biology , arginine , enzyme , escherichia coli , amino acid , polyclonal antibodies , fusion protein , cytoplasm , gene , antibody , genetics , recombinant dna
The lack of knowledge about the tissue and subcellular distribution of polyamines (PAs) and the enzymes involved in their metabolism remains one of the main obstacles in our understanding of the biological role of PAs in plants. Arginine decarboxylase (ADC; EC 4.1.1.9) is a key enzyme in polyamine biosynthesis in plants. We have characterized a cDNA coding for ADC from Nicotiana tabacum L. cv. Petit Havana SR1. The deduced ADC polypeptide had 721 amino acids and a molecular mass of 77 kDa. The ADC cDNA was overexpressed in Escherichia coli , and the ADC fusion protein obtained was used to produce polyclonal antibodies. Using immunological methods, we demonstrate the presence of the ADC protein in all plant organs analysed: flowers, seeds, stems, leaves and roots. Moreover, depending on the tissue, the protein is localized in two different subcellular compartments, the nucleus and the chloroplast. In photosynthetic tissues, ADC is located mainly in chloroplasts, whereas in non‐photosynthetic tissues the protein appears to be located in nuclei. The different compartmentation of ADC may be related to distinct functions of the protein in different cell types.