Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion.
Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion.
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DOI：
10.1016/j.febslet.2012.08.031
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发表时间：
2012-10-19
期刊：
影响因子：
3.5
通讯作者：
Rinehart J
中科院分区：
文献类型：
--
作者：
Heinemann IU;Rovner AJ;Aerni HR;Rogulina S;Cheng L;Olds W;Fischer JT;Söll D;Isaacs FJ;Rinehart J
由UAG密码子编程的遗传编码的磷酸丝氨酸掺入是通过在正常的大肠杆菌翻译机器中添加工程延长因子和古生菌氨基酰tRNA合成酶来实现的(Park(2011)Science 333,1151)。然而，蛋白质产量受到正交磷酸丝氨酸翻译系统的表达和与释放因子1(RF-1)竞争的影响。在缺乏RF-1，磷酸丝氨酸磷酸酶的菌株中，存在于必需基因中的7个UAG密码子被转换为UAA，GFP和WNK4中的磷酸丝氨酸掺入显著增加，但伴随着细胞适合性和活力的丧失。
Genetically encoded phosphoserine incorporation programmed by the UAG codon was achieved by addition of engineered elongation factor and an archaeal aminoacyl-tRNA synthetase to the normal Escherichia coli translation machinery (Park (2011) Science 333, 1151). However, protein yield suffers from expression of the orthogonal phosphoserine translation system and competition with release factor 1 (RF-1). In a strain lacking RF-1, phosphoserine phosphatase, and where 7 UAG codons residing in essential genes were converted to UAA, phosphoserine incorporation into GFP and WNK4 was significantly elevated, but with an accompanying loss in cellular fitness and viability.
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