Protein transport into higher plant peroxisomes - In vitro import assay provides evidence for receptor involvement

被引:26
作者
Brickner, DG
Harada, JJ
Olsen, LJ
机构
[1] UNIV MICHIGAN, DEPT BIOL, ANN ARBOR, MI 48109 USA
[2] UNIV CALIF DAVIS, DIV BIOL SCI, PLANT BIOL SECT, DAVIS, CA 95616 USA
关键词
D O I
10.1104/pp.113.4.1213
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Peroxisome biogenesis requires that proteins be transported from their site of synthesis in the cytoplasm to their final location in the peroxisome matrix or membrane. Glyoxysomes are a class of peroxisomes found primarily in germinating seedlings and are involved in mobilizing fatty acids via the glyoxylate cycle and the beta-oxidation pathway. We have used an in vitro assay to study the mechanism(s) of import of proteins into glyoxysomes. Results from this assay indicate that the transport process is time- and temperature-dependent and is specific for peroxisomal proteins. Isocitrate lyase, a glyoxysomal protein, and the leaf-type peroxisomal enzyme glycolate oxidase (GLO) were transported into pumpkin (Cucurbita pepo) glyoxysomes with no apparent differences in efficiency of import. Thus, this in vitro assay appears to be physiologically relevant and correlates well with expected in vivo conditions. Protein import was also energy-dependent and saturable. Nonradiolabeled GLO competed with radiolabeled, in vitro-synthesized GLO for components of the import machinery. Finally, pretreatment of the isolated glyoxysomes with protease virtually abolished subsequent import of GLO. Taken together, these results indicate that a proteinaceous receptor is involved in the import of peroxisomal proteins.
引用
收藏
页码:1213 / 1221
页数:9
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