Denecke J, Botterman J, Deblaere R
Plant Genetic Systems N.V., Gent, Belgium.
Plant Cell. 1990 Jan;2(1):51-9. doi: 10.1105/tpc.2.1.51.
To study protein secretion in plant cells, we established and evaluated a model system based on transient synthesis of heterologous proteins in tobacco protoplasts. We show that the nonsecretory enzymes phosphinothricin acetyl transferase, neomycin phosphotransferase II, and beta-glucuronidase are secreted when targeted to the lumen of the endoplasmic reticulum by signal peptide-mediated translocation. These data are consistent with the view that secretion can occur independent of active sorting mechanisms by nonspecific migration through the exocytic pathway. However, the rate of secretion differs significantly among these enzymes. Furthermore, the presence of signal sequences was found to be correlated with a reduction of the levels of the encoded gene products. This is the result of post-transcriptional events that limit either synthesis or stability of the proteins in vivo.
为了研究植物细胞中的蛋白质分泌,我们建立并评估了一个基于烟草原生质体中异源蛋白质瞬时合成的模型系统。我们发现,当通过信号肽介导的转运将非分泌性酶草丁膦乙酰转移酶、新霉素磷酸转移酶II和β-葡萄糖醛酸酶靶向内质网腔时,它们会被分泌。这些数据与以下观点一致,即分泌可以通过胞吐途径的非特异性迁移独立于主动分选机制而发生。然而,这些酶之间的分泌速率差异显著。此外,发现信号序列的存在与编码基因产物水平的降低相关。这是转录后事件的结果,这些事件限制了体内蛋白质的合成或稳定性。