Enhancement of soluble protein expression through the use of fusion tags

被引:459
作者
Esposito, Dominic [1 ]
Chatterjee, Deb K. [1 ]
机构
[1] NCI, Res Technol Program, Prot Express Lab, SAIC Frederick Inc, Ft Detrick, MD 21702 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/j.copbio.2006.06.003
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The soluble expression of heterologous proteins in Escherichia coli remains a serious bottleneck in protein production. Although alteration of expression conditions can sometimes solve the problem, the best available tools to date have been fusion tags that enhance the solubility of expressed proteins. However, a systematic analysis of the utility of these solubility fusions has been difficult, and it appears that many proteins react differently to the presence of different solubility tags. The advent of high-throughput structural genomics programs and advances in cloning and expression technology afford us a new way to compare the effectiveness of solubility tags. This data should allow us to better predict the effectiveness of tags currently in use, and might also provide the information needed to identify new fusion tags.
引用
收藏
页码:353 / 358
页数:6
相关论文
共 52 条
[1]   Recombinant protein expression in Escherichia coli [J].
Baneyx, F .
CURRENT OPINION IN BIOTECHNOLOGY, 1999, 10 (05) :411-421
[2]   Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization [J].
Bao, Wen-Jing ;
Gao, Yong-Guang ;
Chang, Yong-Gang ;
Zhang, Tie-Ying ;
Lin, Xiao-Jing ;
Yan, Xian-Zhong ;
Hu, Hong-Yu .
PROTEIN EXPRESSION AND PURIFICATION, 2006, 47 (02) :599-606
[3]   Dual expression system suitable for high-throughput fluorescence-based screening and production of soluble proteins [J].
Braud, S ;
Moutiez, M ;
Belin, P ;
Abello, N ;
Drevet, P ;
Zinn-Justin, S ;
Courçon, M ;
Masson, C ;
Dassa, J ;
Charbonnier, JB ;
Boulain, JC ;
Ménez, A ;
Genet, R ;
Gondry, M .
JOURNAL OF PROTEOME RESEARCH, 2005, 4 (06) :2137-2147
[4]   Construction of a set Gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli [J].
Busso, D ;
Delagoutte-Busso, B ;
Moras, D .
ANALYTICAL BIOCHEMISTRY, 2005, 343 (02) :313-321
[5]   High-throughput screening for soluble recombinant expressed kinases in Escherichia coli and insect cells [J].
Chambers, SP ;
Austen, DA ;
Fulghum, JR ;
Kim, WM .
PROTEIN EXPRESSION AND PURIFICATION, 2004, 36 (01) :40-47
[6]   Enhanced soluble protein expression using two new fusion tags [J].
Chatterjee, DK ;
Esposito, D .
PROTEIN EXPRESSION AND PURIFICATION, 2006, 46 (01) :122-129
[7]   Turning protein crystallisation from an art into a science [J].
Chayen, NE .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2004, 14 (05) :577-583
[8]   An efficient system for small protein expression and refolding [J].
Cheng, Y ;
Patel, DJ .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 317 (02) :401-405
[9]   Expression of heterologous proteins in Pichia pastoris:: a useful experimental tool in protein engineering and production [J].
Daly, R ;
Hearn, MTW .
JOURNAL OF MOLECULAR RECOGNITION, 2005, 18 (02) :119-138
[10]  
Davis GD, 1999, BIOTECHNOL BIOENG, V65, P382, DOI 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.3.CO