Keller G A, Gould S, Deluca M, Subramani S
Proc Natl Acad Sci U S A. 1987 May;84(10):3264-8. doi: 10.1073/pnas.84.10.3264.
Although several enzymes known to reside in peroxisomes have been studied extensively, no cis-acting amino acid sequences involved in the transport of these proteins to peroxisomes have been described. As a first step towards the determination of a putative peroxisomal targeting sequence, we have expressed the cDNA encoding the firefly luciferase [Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolyzing), EC 1.13.12.7] in monkey kidney cells and found that the product of the gene is transported to peroxisomes. Luciferase is derived from the firefly (Photinus pyralis) and is synthesized and stored in the cells of the firefly's lantern organ, where it is also found in peroxisomes. The fact that this protein is similarly targeted in cells from such different organisms suggests that the process of protein transport to peroxisomes has been highly conserved through evolution.
尽管对几种已知存在于过氧化物酶体中的酶进行了广泛研究,但尚未描述参与这些蛋白质向过氧化物酶体转运的顺式作用氨基酸序列。作为确定假定的过氧化物酶体靶向序列的第一步,我们在猴肾细胞中表达了编码萤火虫荧光素酶[Photinus-荧光素:氧4-氧化还原酶(脱羧,ATP水解),EC 1.13.12.7]的cDNA,发现该基因的产物被转运到过氧化物酶体。荧光素酶源自萤火虫(Photinus pyralis),在萤火虫发光器官的细胞中合成并储存,在这些细胞的过氧化物酶体中也能找到。这种蛋白质在如此不同的生物体的细胞中具有相似的靶向性,这一事实表明蛋白质向过氧化物酶体转运的过程在进化过程中得到了高度保守。