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Versatility of Protein Synthesis in a Test Tube

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 343

Special Issue Editor


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Guest Editor
Department of Molecular Biology, Institute of of Biochemistry and Molecular Biology, Semmelweis University, H-1094 Budapest, Hungary
Interests: functional analysis of proteins by in vitro translation; aptamer generation for diagnostic purposes
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The genetic code is manifested in thousands of proteins in all living organisms. Determining the function of these proteins is a challenging task in life sciences. The analysis of individual proteins typically begins with producing the protein of interest, which can often be a bottleneck for further analysis. Although cell cultures are currently the most widely used platforms for recombinant protein production, cell-free translation systems are a more rational approach for small-scale and high-throughput protein synthesis, as well as synthetic biology studies. In recent decades, cell-free translation systems have been optimized for synthesizing difficult-to-produce proteins, such as those with disulfide bridges and membrane proteins, and even for composing functional protein complexes. Recent developments have made cell-free translation an even more versatile method for producing proteins, and it is expected to be the method of choice in an increasing number of laboratories.

This Special Issue aims to provide insight into the current status of cell-free protein production and showcase the capabilities of optimised, next-generation in vitro translation systems.

Dr. Tamás Mészáros
Guest Editor

Manuscript Submission Information

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Keywords

  • protein synthesis
  • synthetic biology
  • cell-free translation
  • in vitro translation

Published Papers (1 paper)

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Research

11 pages, 3554 KiB  
Article
N-Terminal Amino Acid Affects the Translation Efficiency at Lower Temperatures in a Reconstituted Protein Synthesis System
by Tomoe Fuse-Murakami, Rena Matsumoto and Takashi Kanamori
Int. J. Mol. Sci. 2024, 25(10), 5264; https://doi.org/10.3390/ijms25105264 (registering DOI) - 12 May 2024
Viewed by 201
Abstract
The Escherichia coli (E. coli)-based protein synthesis using recombinant elements (PURE) system is a cell-free protein synthesis system reconstituted from purified factors essential for E. coli translation. The PURE system is widely used for basic and synthetic biology applications. One of [...] Read more.
The Escherichia coli (E. coli)-based protein synthesis using recombinant elements (PURE) system is a cell-free protein synthesis system reconstituted from purified factors essential for E. coli translation. The PURE system is widely used for basic and synthetic biology applications. One of the major challenges associated with the PURE system is that the protein yield of the system varies depending on the protein. Studies have reported that the efficiency of translation is significantly affected by nucleotide and amino acid sequences, especially in the N-terminal region. Here, we investigated the inherent effect of various N-terminal sequences on protein synthesis using the PURE system. We found that a single amino acid substitution in the N-terminal region significantly altered translation efficiency in the PURE system, especially at low temperatures. This result gives us useful suggestions for the expression of the protein of interest in vitro and in vivo. Full article
(This article belongs to the Special Issue Versatility of Protein Synthesis in a Test Tube)
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