Fusion tags to enhance heterologous protein expression
- PMID: 31993706
- DOI: 10.1007/s00253-020-10402-8
Fusion tags to enhance heterologous protein expression
Abstract
Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system. Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.
Keywords: Aggregation-prone tag; Escherichia coli; Expression-enhancing tag; Fusion tag; Heterologous protein expression; Inclusion body; Peptide tag; Protein tag; Solubility tag.
Similar articles
-
Expression and Purification of Recombinant Proteins in Escherichia coli with a His6 or Dual His6-MBP Tag.Methods Mol Biol. 2017;1607:1-15. doi: 10.1007/978-1-4939-7000-1_1. Methods Mol Biol. 2017. PMID: 28573567 Free PMC article.
-
A novel protein fusion partner, carbohydrate-binding module family 66, to enhance heterologous protein expression in Escherichia coli.Microb Cell Fact. 2021 Dec 28;20(1):232. doi: 10.1186/s12934-021-01725-w. Microb Cell Fact. 2021. PMID: 34963459 Free PMC article.
-
Application of an E. coli signal sequence as a versatile inclusion body tag.Microb Cell Fact. 2017 Mar 21;16(1):50. doi: 10.1186/s12934-017-0662-4. Microb Cell Fact. 2017. PMID: 28320377 Free PMC article.
-
Enhancing the solubility of recombinant proteins in Escherichia coli by using hexahistidine-tagged maltose-binding protein as a fusion partner.Methods Mol Biol. 2011;705:259-74. doi: 10.1007/978-1-61737-967-3_16. Methods Mol Biol. 2011. PMID: 21125392 Review.
-
In vivo cleavage of solubility tags as a tool to enhance the levels of soluble recombinant proteins in Escherichia coli.Biotechnol Bioeng. 2021 Nov;118(11):4159-4167. doi: 10.1002/bit.27912. Epub 2021 Aug 14. Biotechnol Bioeng. 2021. PMID: 34370304 Review.
Cited by
-
SPI "sandwich": Combined SUMO-Peptide-Intein expression system and isolation procedure for improved stability and yield of peptides.Protein Sci. 2022 May;31(5):e4316. doi: 10.1002/pro.4316. Protein Sci. 2022. PMID: 35481634 Free PMC article.
-
Recombinant expression of hen egg white lysozyme with the assistance of xylanase fusion partner in Pichia pastoris.Bioengineered. 2022 May;13(5):13860-13871. doi: 10.1080/21655979.2022.2084496. Bioengineered. 2022. PMID: 35726822 Free PMC article.
-
The Protocatechuate 3,4-Dioxygenase Solubility (PCDS) Tag Enhances the Expression and Solubility of Heterogenous Proteins in Escherichia coli.Front Microbiol. 2021 Nov 29;12:779541. doi: 10.3389/fmicb.2021.779541. eCollection 2021. Front Microbiol. 2021. PMID: 34912319 Free PMC article.
-
Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8.Microb Cell Fact. 2021 Jan 7;20(1):9. doi: 10.1186/s12934-020-01502-1. Microb Cell Fact. 2021. PMID: 33413407 Free PMC article.
-
Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology.Front Mol Biosci. 2021 Mar 25;8:639587. doi: 10.3389/fmolb.2021.639587. eCollection 2021. Front Mol Biosci. 2021. PMID: 33842544 Free PMC article. Review.
Publication types
MeSH terms
Substances
Grants and funding
- Marine Biomaterials Research Center/a grant from the Marine Biotechnology Program, funded by the Ministry of Oceans and Fisheries, Korea
- NRF-2018R1A6A3A11040793/Research Fellow Funding Grant of NRF
- NRF-2015M1A5A1037054/the Basic Core Technology Development Program for the Oceans and the Polar Regions of the NRF
- Grant/Korea University
LinkOut - more resources
Full Text Sources
Other Literature Sources
