Bedouelle H, Duplay P, Hofnung M
Unité de Biochimie des Régulations cellulaires, C.N.R.S.-U.A. n. 1129, Institut Pasteur, Paris.
C R Acad Sci III. 1987;305(17):623-6.
Enzymes can be fused at the C-terminal end of the maltose binding protein (MalE), at the genetic level. Expression of the hybrid proteins, under control of promoter malEp and of the constitutive activator, MalTc1, can be repressed by glucose. The hybrid proteins are localised either in the bacterial cytoplasm or periplasmic space, depending on whether MalE harbors a signal peptide mutation or not; as MalE, they can be purified in one step by chromatography on cross-linked amylose. The Staphylococcus aureus Nuclease and the Klenow portion of E. coli DNA-polymerase I keep their specific activities when fused to MalE.
在基因水平上，酶可以融合在麦芽糖结合蛋白（MalE）的C末端。在启动子malEp和组成型激活剂MalTc1的控制下，杂合蛋白的表达可以被葡萄糖抑制。根据MalE是否含有信号肽突变，杂合蛋白定位于细菌细胞质或周质空间；与MalE一样，它们可以通过交联直链淀粉柱色谱一步纯化。金黄色葡萄球菌核酸酶和大肠杆菌DNA聚合酶I的Klenow片段与MalE融合时保留其特定活性。
