Conservation of function between mammalian and plant steroid 5 alpha-reductases

被引:123
作者
Li, JM
Biswas, MG
Chao, A
Russell, DW
Chory, J
机构
[1] SALK INST BIOL STUDIES,PLANT BIOL LAB,LA JOLLA,CA 92037
[2] UNIV TEXAS,SW MED CTR,DEPT MOL GENET,DALLAS,TX 75235
关键词
D O I
10.1073/pnas.94.8.3554
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Arabidopsis det2 mutants are small dark-green dwarfs displaying pleiotropic defects in light-regulated development during multiple stages of the plant life cycle. The DET2 gene encodes a protein that shares approximate to 40% sequence identity with mammalian steroid 5 alpha-reductases and is implicated in the synthesis of a class of plant steroids, the brassinosteroids. Here we show that the DET2 protein, when expressed in human embryonic kidney 293 cells, catalyzes the 5 alpha-reduction of several animal steroid substrates and has similar kinetic properties to the mammalian steroid 5 alpha-reductase enzymes. Moreover, human steroid 5 alpha-reductases expressed in det2 mutant plants can substitute for DET2 in brassinosteroid biosynthesis. These data indicate that DETZ is an ortholog of the mammalian steroid 5 alpha-reductases and provide further evidence that brassinosteroids play an essential role in light-regulated plant development. The structural and functional conservation between DET and human steroid 5 alpha-reductases raise interesting issues concerning the evolutionary origin of the steroid hormone signaling system.
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页码:3554 / 3559
页数:6
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