Endogenous Level of 28-Norcastasterone Is Strictly Regulated in Plant Cells

A cell-free enzyme solution prepared from cultured cells of Phaseolus vulgaris mediated C-24 methylation of 28-nor­castasterone 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-norcastas...

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Bibliographic Details
Published in:Journal of plant biology = Singmul Hakhoe chi Vol. 48; no. 4; pp. 483 - 486
Main Authors: Kim Tae-Wuk, Hwang Jung-Yun, Joo Se-Hwan, Cheong Hyeonsook, Pharis Richard P, Kim Seong-Ki
Format: Journal Article
Language:Korean
Published: 2005
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Summary:A cell-free enzyme solution prepared from cultured cells of Phaseolus vulgaris mediated C-24 methylation of 28-nor­castasterone 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 28­norcastasterone, along with castasterone and brassinolide, is an important brassinosteroid whose endogenous level should be strictly controlled to express brassinosteroid activities in plants.
Bibliography:KISTI1.1003/JNL.JAKO200509408764683
ISSN:1226-9239
1867-0725