Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli

被引：86
|
作者：
Johnson, Matthew [1 ]
Coulton, Arthur T. [1 ]
Geeves, Michael A. [1 ]
Mulvihill, Daniel P. [1 ]
机构：
[1] Univ Kent, Sch Biosci, Canterbury, Kent, England
来源：
PLOS ONE | 2010年 / 5卷 / 12期
基金：
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词：
TROPOMYOSIN FUNCTION; YEAST; ACTIN; ACETYLTRANSFERASE;
D O I：
10.1371/journal.pone.0015801
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
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页数：5
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