Targeted amino-terminal acetylation of recombinant proteins in E. coli.
Targeted amino-terminal acetylation of recombinant proteins in E. coli.
复制标题
DOI：
10.1371/journal.pone.0015801
复制
发表时间：
2010-12-23
期刊：
影响因子：
3.7
通讯作者：
Mulvihill DP
中科院分区：
文献类型：
--
作者：
Johnson M;Coulton AT;Geeves MA;Mulvihill DP
细菌中真核蛋白表达的一个主要限制是无法对表达的蛋白进行翻译后修饰。氨基末端乙酰化是一种对蛋白质功能至关重要的修饰。通过在大肠杆菌中共表达裂殖酵母 NatB 复合物与目标蛋白，我们报道了一种简单且广泛适用的表达和纯化功能性 N 末端乙酰化真核蛋白的方法。
One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co-expressing the fission yeast NatB complex with the target protein in E.coli, we report a simple and widely applicable method for the expression and purification of functional N-terminally acetylated eukaryotic proteins.