The rhal gene from Arabidopsis encodes a small GTP binding protein belonging to the YpVRab family. Transgenic Arabidop-sis plants containing the promoter region of the rhal gene fused to the P-glucuronidase (gus) reporter gene revealed gus expression limited mainly to the guard cells of stomata, the stipules, and the mot tip of young plants. In flowering plants, expression was found predominantly in the receptacle and in guard cells of the different flower organs. High GUS activity could also be seen in callus tissue and developing seeds. No detectable activity was present in other plant tissues ; activity could not be induced by various treatments. GUS activity was visualized histochemically using both 5-bromo-4-chloro-3-indolyl P-D-glucuronide and a newly developed GUS substrate: Sudan Il-8-glucuronide. The latter precipitates as red crystals at the site of GUS activity. Results obtained by the gus analysis were confirmed by whole-mount mRNA in situ hybridization. A hypothesis for the function of the Rhal protein is discussed.
In the search of heterocyclic ring systems potentially useful as α-glucosidase inhibitors we have synthesized a set of heterocycles bearing hydroacridone 4-5, hydroxanthone 6, quinazolone 8, benzoyl phtalimide 9 and isoquinolone 10-11. These compounds under study were subjected to enzyme inhibition and compared against reference inhibitor acarbose observing potent inhibition for benzoyl phtalimide 9, and isoquinolone dione 11. Based on their inhibition activity, both candidates were selected for docking analysis to determine their best posing, and the interactions involved between the ligand and the residues. A comparative analysis was established to determine the potential correlation between the interactions found, the inhibition observed for the candidates and the interactions observed for the reference inhibitor acarbose.
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