Literature DB >> 20349333

N-terminally truncated GADD34 proteins are convenient translation enhancers in a human cell-derived in vitro protein synthesis system.

Satoshi Mikami1, Tominari Kobayashi, Kodai Machida, Mamiko Masutani, Shigeyuki Yokoyama, Hiroaki Imataka.   

Abstract

Human cell-derived in vitro protein synthesis systems are useful for the production of recombinant proteins. Productivity can be increased by supplementation with GADD34, a protein that is difficult to express in and purify from E. coli. Deletion of the N-terminal 120 or 240 amino acids of GADD34 improves recovery of this protein from E. coli without compromising its ability to boost protein synthesis in an in vitro protein synthesis system. The use of N-terminally truncated GADD34 proteins in place of full-length GADD34 should improve the utility of human cell-based cell-free protein synthesis systems.

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Year:  2010        PMID: 20349333     DOI: 10.1007/s10529-010-0251-7

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  8 in total

1.  Engineering artificial cells by combining HeLa-based cell-free expression and ultrathin double emulsion template.

Authors:  Kenneth K Y Ho; Victoria L Murray; Allen P Liu
Journal:  Methods Cell Biol       Date:  2015-04-08       Impact factor: 1.441

2.  Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable: achieving specificity by targeting substrate and regulatory protein interaction sites.

Authors:  Wolfgang Peti; Rebecca Page
Journal:  Bioorg Med Chem       Date:  2015-02-26       Impact factor: 3.641

3.  A translation system reconstituted with human factors proves that processing of encephalomyocarditis virus proteins 2A and 2B occurs in the elongation phase of translation without eukaryotic release factors.

Authors:  Kodai Machida; Satoshi Mikami; Mamiko Masutani; Kurumi Mishima; Tominari Kobayashi; Hiroaki Imataka
Journal:  J Biol Chem       Date:  2014-09-25       Impact factor: 5.157

4.  N1-methyl-pseudouridine in mRNA enhances translation through eIF2α-dependent and independent mechanisms by increasing ribosome density.

Authors:  Yuri V Svitkin; Yi Min Cheng; Tirtha Chakraborty; Vladimir Presnyak; Matthias John; Nahum Sonenberg
Journal:  Nucleic Acids Res       Date:  2017-06-02       Impact factor: 16.971

5.  Design, Development and Optimization of a Functional Mammalian Cell-Free Protein Synthesis Platform.

Authors:  Chiara Heide; Gizem Buldum; Ignacio Moya-Ramirez; Oscar Ces; Cleo Kontoravdi; Karen M Polizzi
Journal:  Front Bioeng Biotechnol       Date:  2021-02-02

6.  Production of human translation-competent lysates using dual centrifugation.

Authors:  Lukas-Adrian Gurzeler; Jana Ziegelmüller; Oliver Mühlemann; Evangelos D Karousis
Journal:  RNA Biol       Date:  2021-12-29       Impact factor: 4.652

Review 7.  Cell-Free Protein Synthesis: Pros and Cons of Prokaryotic and Eukaryotic Systems.

Authors:  Anne Zemella; Lena Thoring; Christian Hoffmeister; Stefan Kubick
Journal:  Chembiochem       Date:  2015-10-19       Impact factor: 3.461

8.  A Sephin1-insensitive tripartite holophosphatase dephosphorylates translation initiation factor 2α.

Authors:  Ana Crespillo-Casado; Zander Claes; Meng S Choy; Wolfgang Peti; Mathieu Bollen; David Ron
Journal:  J Biol Chem       Date:  2018-04-04       Impact factor: 5.157

  8 in total

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