Gould S J, Keller G A, Schneider M, Howell S H, Garrard L J, Goodman J M, Distel B, Tabak H, Subramani S
Department of Biology, University of California, La Jolla 92093.
EMBO J. 1990 Jan;9(1):85-90. doi: 10.1002/j.1460-2075.1990.tb08083.x.
We have previously demonstrated that firefly luciferase can be imported into peroxisomes of both insect and mammalian cells. To determine whether the process of protein transport into the peroxisome is functionally similar in more widely divergent eukaryotes, the cDNA encoding firefly luciferase was expressed in both yeast and plant cells. Luciferase was translocated into peroxisomes in each type of organism. Experiments were also performed to determine whether a yeast peroxisomal protein could be transported to peroxisomes in mammalian cells. We observed that a C-terminal segment of the yeast (Candida boidinii) peroxisomal protein PMP20 could act as a peroxisomal targeting signal in mammalian cells. These results suggest that at least one mechanism of protein translocation into peroxisomes has been conserved throughout eukaryotic evolution.
我们之前已经证明,萤火虫荧光素酶能够导入昆虫和哺乳动物细胞的过氧化物酶体。为了确定在差异更大的真核生物中,蛋白质转运到过氧化物酶体的过程在功能上是否相似,编码萤火虫荧光素酶的cDNA在酵母和植物细胞中均有表达。荧光素酶在每种生物体中都被转运到过氧化物酶体中。还进行了实验以确定酵母过氧化物酶体蛋白是否能转运到哺乳动物细胞的过氧化物酶体中。我们观察到酵母(博伊丁假丝酵母)过氧化物酶体蛋白PMP20的C末端片段可作为哺乳动物细胞中的过氧化物酶体靶向信号。这些结果表明,至少一种蛋白质转运到过氧化物酶体的机制在整个真核生物进化过程中得以保留。