Caged phosphoproteins
Caged phosphoproteins
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DOI：
10.1021/ja043875c
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发表时间：
2005-01-26
影响因子：
15
通讯作者：
Imperiali, B
中科院分区：
文献类型：
--
作者：
Rothman, DM;Petersson, EJ;Imperiali, B
我们目前的化学和生物合成的笼磷蛋白在体外无义密码子抑制方法。具体而言，合成了丝氨酸、苏氨酸和酪氨酸的磷酸氨基酸类似物，其具有单个可光裂解的o-硝基苯乙基笼状基团，作为用于插入全长蛋白质的氨酰tRNA加合物。为此，开发了一种新型亚磷酸化试剂。报道了利用体外翻译系统将这些大体积的带电荷的氨基酸成功地掺入烟碱乙酰胆碱受体（nAChR）和血管舒张刺激磷蛋白（VASP）的α亚基中。
We present the chemical and biological synthesis of caged phosphoproteins using the in vitro nonsense codon suppression methodology. Specifically, phosphoamino acid analogues of serine, threonine, and tyrosine with a single photocleavableo-nitrophenylethyl caging group were synthesized as the amino acyl tRNA adducts for insertion into full-length proteins. For this purpose, a novel phosphitylating agent was developed. The successful incorporation of these bulky and charged amino acids into the α-subunit of the nicotinic acetyl choline receptor (nAChR) and the vasodilator-stimulated phosphoprotein (VASP) using an in vitro translation system is reported.