The Study of Different Signal Peptides in Improvement of Recombinant Proteins Solubility in E. coli: A Mini-Review Article

被引：0
作者：
Rahmatabadi, Seyyed Soheil [1 ,2 ]
Askari, Soudabeh [3 ]
Khademi, Fatemeh [2 ]
Soleymani, Bijan [2 ]
机构：
[1] Kermanshah Univ Med Sci, Hlth Technol Inst, Nano Drug Delivery Res Ctr, Kermanshah, Iran
[2] Kermanshah Univ Med Sci, Hlth Technol Inst, Med Biol Res Ctr, Kermanshah, Iran
[3] Appl Razi Biotechnol, Kermanshah, Iran
来源：
CURRENT PROTEOMICS | 2024年 / 21卷 / 03期
关键词：
Inclusion bodies; solubility; signal peptide; recombinant protein; expression; E; coli; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; EXTRACELLULAR PRODUCTION; HETEROLOGOUS PROTEINS; SECRETORY EXPRESSION; POSITIVE CHARGE; DISULFIDE BONDS; TAC PROMOTER; MEMBRANE; OPTIMIZATION;
D O I：
10.2174/0115701646305738240730113619
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
In E. coli, the production of proteins as inclusion bodies (IBs) caused a decrease in the solubility and activity of these products. Diverse approaches and methods have been used by investigators to overcome this problem. The secretion of recombinant proteins into the periplasmic space by means of suitable signal peptides is a way to resolve these limitations for the production of recombinant proteins in a native form. Secretory production of recombinant proteins in bacterial hosts has many advantages and thus, it is a topic of interest. However, it is hard to achieve due to the difficulty of the process and the need for the choice of appropriate signal peptide for each host and protein. Based on the literature, different signal peptides have experimentally been applied to enhance the solubility of various recombinant proteins. It has been shown that the secretion efficiency of a given protein differs dramatically based on the type of the signal peptide that is attached to the protein. Therefore, the choice and alteration of signal peptides are the two crucial approaches for the improvement of a recombinant protein secretion that have been discussed in this review. Also, different factors affecting the expression and solubility of recombinant proteins have been discussed.
引用
收藏
页码：129 / 139
页数：11
相关论文
共 108 条
[1]   Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli [J].
Alami, M ;
Lüke, I ;
Deitermann, S ;
Eisner, G ;
Koch, HG ;
Brunner, J ;
Müller, M .
MOLECULAR CELL, 2003, 12 (04) :937-946
[2]   Recombinant protein folding and misfolding in Escherichia coli [J].
Baneyx, F ;
Mujacic, M .
NATURE BIOTECHNOLOGY, 2004, 22 (11) :1399-1408
[3]   Isolation and characterization of the E-coli membrane protein production strain Mutant56(DE3) [J].
Baumgarten, Thomas ;
Schlegel, Susan ;
Wagner, Samuel ;
Low, Mirjam ;
Eriksson, Jonas ;
Bonde, Ida ;
Herrgard, Markus J. ;
Heipieper, Hermann J. ;
Norholm, Morten H. H. ;
Slotboom, Dirk Jan ;
de Gier, Jan-Willem .
SCIENTIFIC REPORTS, 2017, 7
[4]   SecB-A chaperone dedicated to protein translocation [J].
Bechtluft, Philipp ;
Nouwen, Nico ;
Tans, Sander J. ;
Driessen, Arnold J. M. .
MOLECULAR BIOSYSTEMS, 2010, 6 (04) :620-627
[5]   Effect of signal peptide on the stability and folding kinetics of maltose binding protein [J].
Beena, K ;
Udgaonkar, JB ;
Varadarajan, R .
BIOCHEMISTRY, 2004, 43 (12) :3608-3619
[6]  
Boock JT, 2015, METHODS MOL BIOL, V1258, P79, DOI 10.1007/978-1-4939-2205-5_5
[7]  
BROSIUS J, 1985, J BIOL CHEM, V260, P3539
[8]   An investigation into the pathogenic properties of Escherichia coli strains BLR, BL21, DH5α and EQ1 [J].
Chart, H ;
Smith, HR ;
La Ragione, RM ;
Woodward, MJ .
JOURNAL OF APPLIED MICROBIOLOGY, 2000, 89 (06) :1048-1058
[9]  
Chen JQ, 2002, J MOL MICROB BIOTECH, V4, P519
[10]  
CHOU MM, 1990, J BIOL CHEM, V265, P2873
12345678910