CECCHINI NICOLÁS MIGUEL
Congresos y reuniones científicas
Título:
TOWARDS FUNCTIONALCHARACTERIZATION OFTHE PROLINE DEHYDROGENASE ISOFORMS INTHE PLANT DEFENCE
Autor/es:
RIZZI YS; CECCHINI NM; ÁLVAREZ ME
Reunión:
Congreso; SAIB - 48 Annual Meeting XLVIII Reunión Anual th Argentine Society for Biochemistry and Molecular Biology Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2012
Resumen:
ProDH is the first of two enzymes involved in the oxidation ofproline into glutamic acid. In plants, the enzyme is required fornormal development of the Hypersensitive Response, a defenseagainst biotrophic pathogens. The Arabidopsis ProDH isoforms,ProDH1 and ProDH2, differ in some physiological functions.and genes contain elements mediatingresponses to salcylic acid (SA) and jasmonic acid (JA). However,their differential sensitivity to infections inducing these pathwaysremains unknown. To start evaluating this point we treated plantswith pathogens or hormones. In wild type plants the infection withAvr-Rpm1 induced both genes, whereas SAand JAgenerated differential effects on their expression. In contrast,in and mutants impaired in the SA or JA pathways, thispathogen stimulated abnormal responses for andwith differences among both kind of mutants. Besides, wasinduced by the necrotrophic pathogen . Theseresults suggest that both ProDH isoforms may contribute topathogen resistance under different infection conditions, probablyby displaying non-redundant functions in plant immunity.