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Abstract
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The Arabidopsis deetiolated2 mutant is blocked early in brassinosteroid biosynthesis.

S Fujioka, J Li, Y H Choi, H Seto, S Takatsuto, T Noguchi, T Watanabe, H Kuriyama, T Yokota, J Chory, A Sakurai
S Fujioka
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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J Li
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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Y H Choi
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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H Seto
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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S Takatsuto
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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T Noguchi
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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T Watanabe
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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H Kuriyama
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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T Yokota
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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J Chory
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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A Sakurai
Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
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Published November 1997. DOI: https://doi.org/10.1105/tpc.9.11.1951

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Abstract

The Arabidopsis DEETIOLATED2 (DET2) gene has been cloned and shown to encode a protein that shares significant sequence identity with mammalian steroid 5 alpha-reductases. Loss of DET2 function causes many defects in Arabidopsis development that can be rescued by the application of brassinolide; therefore, we propose that DET2 encodes a reductase that acts at the first step of the proposed biosynthetic pathway--in the conversion of campesterol to campestanol. Here, we used biochemical measurements and biological assays to determine the precise biochemical defect in det2 mutants. We show that DET2 actually acts at the second step in brassinolide biosynthesis in the 5 alpha-reduction of (24R)-24-methylcholest-4-en-3-one, which is further modified to form campestanol. In feeding experiments using 2H6-labeled campesterol, no significant level of 2H6-labeled campestanol was detected in det2, whereas the wild type accumulated substantial levels. Using gas chromatography-selected ion monitoring analysis, we show that several presumed null alleles of det2 accumulated only 8 to 15% of the wild-type levels of campestanol. Moreover, in det2 mutants, the endogenous levels of (24R)-24-methylcholest-4-en-3-one increased by threefold, whereas the levels of all other measured brassinosteroids accumulated to < 10% of wild-type levels. Exogenously applied biosynthetic intermediates of brassinolide were found to rescue both the dark- and light-grown defects of det2 mutants. Together, these results refine the original proposed pathway for brassinolide and indicate that mutations in DET2 block the second step in brassinosteroid biosynthesis. These results reinforce the utility of combining genetic and biochemical analyses to studies of biosynthetic pathways and strengthen the argument that brassinosteroids play an essential role in Arabidopsis development.

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The Arabidopsis deetiolated2 mutant is blocked early in brassinosteroid biosynthesis.
S Fujioka, J Li, Y H Choi, H Seto, S Takatsuto, T Noguchi, T Watanabe, H Kuriyama, T Yokota, J Chory, A Sakurai
The Plant Cell Nov 1997, 9 (11) 1951-1962; DOI: 10.1105/tpc.9.11.1951

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The Arabidopsis deetiolated2 mutant is blocked early in brassinosteroid biosynthesis.
S Fujioka, J Li, Y H Choi, H Seto, S Takatsuto, T Noguchi, T Watanabe, H Kuriyama, T Yokota, J Chory, A Sakurai
The Plant Cell Nov 1997, 9 (11) 1951-1962; DOI: 10.1105/tpc.9.11.1951
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The Plant Cell
Vol. 9, Issue 11
Nov 1997
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