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Çѱ¹½Ä¹°ÇÐȸ / v.48, no.4, 2005³â, pp.483-486

( Endogenous Level of 28-Norcastasterone Is Strictly Regulated in Plant Cells )
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A cell-free enzyme solution prepared from cultured cells of Phaseolus vulgaris mediated C-24 methylation of 28-nor¡©castasterone to castasterone with the aid of S-adenosylmethionine as a co-substrate in the presence of the NADPH cofactor. This enzyme solution also catalyzed conversion of 28-norcastasterone to a de methylated 28-norcastasterone, most likely 26,28-didemethyl-castasterone, when S-adenosylmethionine was not added to the enzyme solution. Furthermore, gene expression of Arabidopsis CYP85A1 and CYP85A2 mediating the conversion of 6-deoxo-28-norcastasterone to 28-norcastasterone was strongly inhibited by treatment of 28-norcastasterone. These results suggest that 28¡©norcastasterone, along with castasterone and brassinolide, is an important brassinosteroid whose endogenous level should be strictly controlled to express brassinosteroid activities in plants.
 
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Arabidopsis;brassinosteroid;homeostatic regulation;28-norcastasterone;Phaseolus vulgaris;
 
Journal of Plant Biology / v.48, no.4, 2005³â, pp.483-486
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ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200509408764683)
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