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.

引用

页数：5

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