PURE technology
- PMID: 20204844
- DOI: 10.1007/978-1-60327-331-2_2
PURE technology
Abstract
The Escherichia coli-based reconstituted cell-free protein synthesis system, which we named the PURE (Protein synthesis Using Recombinant Elements) system, provides several advantages compared with the conventional cell-extract-based system. Stability of RNA or protein is highly improved because of the lack of harmful degradation enzymes. The system can be easily engineered according to purposes or the proteins to be synthesized, by manipulating the components in the system. In this chapter, we describe the construction and exploitation of the PURE system. Methods for preparing and assembling the components composing the PURE system for the protein synthesis reaction are shown.
Similar articles
-
Ribosome display with the PURE technology.Methods Mol Biol. 2010;607:219-25. doi: 10.1007/978-1-60327-331-2_18. Methods Mol Biol. 2010. PMID: 20204860
-
Cell-free protein production system with the E. coli crude extract for determination of protein folds.Methods Mol Biol. 2010;607:101-11. doi: 10.1007/978-1-60327-331-2_10. Methods Mol Biol. 2010. PMID: 20204852
-
Cell-free protein preparation through prokaryotic transcription-translation methods.Methods Mol Biol. 2010;607:1-10. doi: 10.1007/978-1-60327-331-2_1. Methods Mol Biol. 2010. PMID: 20204843
-
[In vitro protein synthesis system: PURESYSTEM--completely reconstituted system derived from Escherichia coli].Tanpakushitsu Kakusan Koso. 2004 Aug;49(11 Suppl):1520-6. Tanpakushitsu Kakusan Koso. 2004. PMID: 15376968 Review. Japanese. No abstract available.
-
Optimizing scaleup yield for protein production: Computationally Optimized DNA Assembly (CODA) and Translation Engineering.Biotechnol Annu Rev. 2007;13:27-42. doi: 10.1016/S1387-2656(07)13002-7. Biotechnol Annu Rev. 2007. PMID: 17875472 Review.
Cited by
-
Improved cell-free RNA and protein synthesis system.PLoS One. 2014 Sep 2;9(9):e106232. doi: 10.1371/journal.pone.0106232. eCollection 2014. PLoS One. 2014. PMID: 25180701 Free PMC article.
-
De novo expression and antibacterial potential of four lactoferricin peptides in cell-free protein synthesis system.Biotechnol Rep (Amst). 2020 Dec 26;29:e00583. doi: 10.1016/j.btre.2020.e00583. eCollection 2021 Mar. Biotechnol Rep (Amst). 2020. PMID: 33425692 Free PMC article.
-
Reconstitution of Mammalian Mitochondrial Translation System Capable of Long Polypeptide Synthesis.Methods Mol Biol. 2023;2661:233-255. doi: 10.1007/978-1-0716-3171-3_14. Methods Mol Biol. 2023. PMID: 37166641
-
Mechanistic basis for a molecular triage reaction.Science. 2017 Jan 20;355(6322):298-302. doi: 10.1126/science.aah6130. Science. 2017. PMID: 28104892 Free PMC article.
-
Mechanism of client selection by the protein quality-control factor UBE2O.Nat Struct Mol Biol. 2022 Aug;29(8):774-780. doi: 10.1038/s41594-022-00807-6. Epub 2022 Aug 1. Nat Struct Mol Biol. 2022. PMID: 35915257 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources