Characterization of the two arginine decarboxylase (polyamine biosynthesis) paralogues of the endemic subantarctic cruciferous species Pringlea antiscorbutica and analysis of their differential expression during development and response to environmental stress.

Arginine decarboxylase (ADC) is a key enzyme involved in the synthesis of polyamines, which have been implicated in developmental processes and stress responses in higher plants. An ancestral ADC gene appears to have been duplicated at the origin of the Brassicaceae family, thus yielding two paralogues in the derived taxa. ADC gene structure was investigated in Pringlea antiscorbutica R. Br., a geographically isolated Brassicaceae species that is endemic from the subantarctic region. P. antiscorbutica exhibits several biochemical and physiological adaptations related to this cold and harsh environment, including high levels of polyamines, which is unusual in higher plants, and especially high levels of agmatine, the product of the ADC-catalysed reaction. Various ADC clones were obtained from P. antiscorbutica. Sequence and phylogenetic analysis showed that all these clones fitted with the presence of two paralogues, PaADC1 and PaADC2, in P. antiscorbutica. Expression of these ADC paralogues was analyzed in P. antiscorbutica during vegetative development and response to stress. Whereas PaADC2 was expressed at both seedling and mature stages, PaADC1 transcripts were hardly detected during early development and were significantly expressed in mature plants. Moreover, PaADC2, but not PaADC1, expression was up-regulated in response to chilling and salt stress at seedling stage. Analysis of 5' regulatory regions of these ADC genes revealed several differences in putative cis-regulatory elements, which could be associated with specific expression patterns. These results were compared to ADC paralogue expression in Arabidopsis thaliana and are discussed in the evolutionary context of genetic diversity resulting from gene duplication.