Dierks T, Lecca M R, Schmidt B, von Figura K
Institut für Biochemie und Molekulare Zellbiologie, Abt. Biochemie II, Universität Göttingen, Germany.
FEBS Lett. 1998 Feb 13;423(1):61-5. doi: 10.1016/s0014-5793(98)00065-9.
Sulfatases undergo an unusual protein modification leading to conversion of a specific cysteine residue into alpha-formylglycine. This conversion is essential for catalytic activity. In arylsulfatase A the alpha-formylglycine is generated inside the endoplasmic reticulum at a late stage of protein translocation. Using in vitro translation in the presence of transport-competent microsomes we found that arylsulfatase B is also modified in a similar way by the formylglycine-generating machinery. Modification depended on protein transport and on the correct position of the relevant cysteine. Arylsulfatase A and B did not compete for modification, as became apparent in co-expression experiments. This could argue for an association of the modification machinery with the protein translocation apparatus.
硫酸酯酶会经历一种不寻常的蛋白质修饰，导致特定的半胱氨酸残基转化为α-甲酰甘氨酸。这种转化对于催化活性至关重要。在芳基硫酸酯酶A中，α-甲酰甘氨酸是在蛋白质转运的后期在内质网内生成的。利用在具有转运能力的微粒体存在下的体外翻译，我们发现芳基硫酸酯酶B也以类似的方式被甲酰甘氨酸生成机制修饰。修饰依赖于蛋白质转运以及相关半胱氨酸的正确位置。在共表达实验中很明显，芳基硫酸酯酶A和B不会竞争修饰。这可能表明修饰机制与蛋白质转运装置相关联。
