In vitro virus: Bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
In vitro virus: Bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
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DOI：
10.1016/s0014-5793(97)01026-0
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发表时间：
1997-09-08
期刊：
影响因子：
3.5
通讯作者：
Yanagawa, H
中科院分区：
文献类型：
--
作者：
Nemoto, N;MiyamotoSato, E;Yanagawa, H
在进化分子工程中，将基因型分配到表型是必要的。在这项研究中，进行了“体外病毒”的构建，其中基因型分子（mRNA）通过核糖体上的嘌呤霉素在无细胞翻译系统中与表型分子（蛋白质）共价结合。结合效率类似于10%，因此表明体外病毒群体具有类似于10（12）个蛋白变体，该数目是噬菌体展示中的10（4）个。体外病毒可用于检测试管中的蛋白质进化，结果可能作为选择具有最理想功能的蛋白质的一般方法的基础。(C)1997年欧洲生物化学学会联合会。
Adequate means for genotype assignment to phenotype is essential in evolutionary molecular engineering. In this study, construction of 'in vitro virus' was carried out in which a genotype molecule (mRNA) covalently binds to the phenotype molecule (protein) through puromycin on the ribosome in a cell-free translation system. Bonding efficiency was similar to 10%, thus indicating a population of the in vitro virus to have similar to 10(12) protein variants, this number being 10(4) that in the phage display. The in vitro virus is useful for examining protein evolution in a test tube and the results may possibly serve as basis for a general method for selecting proteins possessing the most desirable functions. (C) 1997 Federation of European Biochemical Societies.