Caracterización preliminar de una Ferredoxina Reductasa Putativa como posible candidata para la actividad de Dihidropirimidina Deshidrogenasa (DHPD) en Oryza Sativa L.

Abstract

Rice (Oryza sativa L) is one of the most consumed cereal crops worldwide, being one of the most important food sources (FAO, 2004). This crop is often affected by the different environmental conditions generated by climate change. One of these conditions is the high concentration of salts, present in the growth medium of the plant, producing different physiological and biochemical responses, as mechanisms of tolerance to these adverse conditions. In 2009, Liu and collaborators showed that one of the enzymes involved in resistance to stress by salinity is Dihydropyrimidine Dehydrogenase (DHPD), from the degradation pathway of pyrimidines. The sequence of the DHPDs in mammals is constituted by 5 domains, containing, among others, NADPH, FAD binding sites and Fe/S clusters, found mainly in the N-Terminal (Dobritzsch et al., 2002). But the sequence of the DHPD enzyme in the O. sativa species is shorter, noting the lack of these domains. Therefore, this work seeks to obtain the putative ferredoxin reductase "Fruit Protein" as a possible candidate to the complementary subunit of OsDHPD, since it presents NADPH and FAD binding sites. On the other hand, it was sought to standardize the optimum conditions of rice growth up to the state of seedling at 17 days post-germination, in order to expose different varieties to stress by salts.