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Regulation of arginine decarboxylase by spermine in osmotically‐stressed oat leaves
Author(s) -
Borrell A.,
Besford R. T.,
Altabella T.,
Masgrau C.,
Tiburcio A. F.
Publication year - 1996
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.1399-3054.1996.tb00680.x
Subject(s) - arginine decarboxylase , spermine , putrescine , spermidine , biochemistry , ornithine decarboxylase , avena , enzyme , polyamine , biosynthesis , chemistry , biology , botany
Biosynthesis of polyamines in plants is controlled primarily by the enzymes ornithine decarboxylase (EC 4.1.1.17) and arginine decarboxylase (ADC: EC 4.1.1.19), which are responsible for the production of putrescine, and S ‐adenosyl‐L‐methionine (SAM) decarboxylase (EC 4.1.1.50) that is necessary for the formation of spermidine and spermine (Spm). Little is known about the metabolic or molecular mechanisms regulating the synthesis of these enzymes. We have studied the regulation of ADC synthesis by Spm in osmotically‐stressed oat ( Avena sativa L. ev. Victory) leaves, using a polyclonal antibody to oat ADC and a cDNA clone encoding oat ADC. Treatment with Spm in combination with osmotic stress resulted in increased steady‐state levels of ADC mRNA, yet the levels of ADC activity decreased. This absence of correlation is explained by the fact that Spm inhibits processing of the ADC proenzyme, which results in increased levels of this inactive ADC form and a consequent decrease in the ADC‐processed form. Spermine treatment leads to delayed loss of chlorophyll in dark‐incubated and osmotically‐treated oat leaves. Thus, post‐translational regulation of ADC synthesis by Spm may be important in explaining its anti‐senescence properties.