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Versatility of Protein Synthesis in a Test Tube
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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: 20 February 2025 | Viewed by 5189

Special Issue Editor

Dr. Tamás Mészáros

E-Mail Website
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

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Keywords

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

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Published Papers (4 papers)

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Research

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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 - 12 May 2024
Cited by 1 | Viewed by 1715
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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Review

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19 pages, 1606 KiB  
Review
Circumventing the Impossible: Cell-Free Synthesis of Protein Toxins for Medical and Diagnostic Applications
by Alina Mai Woelbern and Franziska Ramm
Int. J. Mol. Sci. 2024, 25(24), 13293; https://doi.org/10.3390/ijms252413293 - 11 Dec 2024
Viewed by 570
Abstract
Naturally occurring protein toxins can derive from bacteria, fungi, plants, and animal venom. Traditionally, toxins are known for their destructive effects on host cells. Despite, and sometimes even because of, these harmful effects, toxins have been used for medical benefits. The prerequisite for [...] Read more.
Naturally occurring protein toxins can derive from bacteria, fungi, plants, and animal venom. Traditionally, toxins are known for their destructive effects on host cells. Despite, and sometimes even because of, these harmful effects, toxins have been used for medical benefits. The prerequisite for the development of toxin-based medications or treatments against toxins is thorough knowledge about the toxin and its underlying mechanism of action. Thus, the toxin of interest must be synthesized. Traditional cell-based production requires high laboratory safety standards and often results in a low total protein yield due to the toxin’s harmful, cytotoxic nature. These drawbacks can be circumvented by using cell-free protein synthesis (CFPS), a highly adaptable platform technology relying on cell lysates rather than living cells. This review discusses the current advances in cell-free synthesis of protein toxins as well as their uses and applications for pharmaceutical and diagnostic purposes. Full article
(This article belongs to the Special Issue Versatility of Protein Synthesis in a Test Tube)
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27 pages, 5112 KiB  
Review
Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics
by Hyeongwoo Park, Haneul Jin, Dayeong Kim and Joongoo Lee
Int. J. Mol. Sci. 2024, 25(16), 9109; https://doi.org/10.3390/ijms25169109 - 22 Aug 2024
Viewed by 1512
Abstract
Peptide-based antibiotics (PBAs), including antimicrobial peptides (AMPs) and their synthetic mimics, have received significant interest due to their diverse and unique bioactivities. The integration of high-throughput sequencing and bioinformatics tools has dramatically enhanced the discovery of enzymes, allowing researchers to identify specific genes [...] Read more.
Peptide-based antibiotics (PBAs), including antimicrobial peptides (AMPs) and their synthetic mimics, have received significant interest due to their diverse and unique bioactivities. The integration of high-throughput sequencing and bioinformatics tools has dramatically enhanced the discovery of enzymes, allowing researchers to identify specific genes and metabolic pathways responsible for producing novel PBAs more precisely. Cell-free systems (CFSs) that allow precise control over transcription and translation in vitro are being adapted, which accelerate the identification, characterization, selection, and production of novel PBAs. Furthermore, these platforms offer an ideal solution for overcoming the limitations of small-molecule antibiotics, which often lack efficacy against a broad spectrum of pathogens and contribute to the development of antibiotic resistance. In this review, we highlight recent examples of how CFSs streamline these processes while expanding our ability to access new antimicrobial agents that are effective against antibiotic-resistant infections. Full article
(This article belongs to the Special Issue Versatility of Protein Synthesis in a Test Tube)
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Other

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8 pages, 837 KiB  
Brief Report
Venom Ex Machina? Exploring the Potential of Cell-Free Protein Production for Venom Biodiscovery
by Anne Paas, Josephine Dresler, Lea Talmann, Andreas Vilcinskas and Tim Lüddecke
Int. J. Mol. Sci. 2024, 25(15), 8286; https://doi.org/10.3390/ijms25158286 - 29 Jul 2024
Cited by 1 | Viewed by 889
Abstract
Venoms are a complex cocktail of potent biomolecules and are present in many animal lineages. Owed to their translational potential in biomedicine, agriculture and industrial applications, they have been targeted by several biodiscovery programs in the past. That said, many venomous animals are [...] Read more.
Venoms are a complex cocktail of potent biomolecules and are present in many animal lineages. Owed to their translational potential in biomedicine, agriculture and industrial applications, they have been targeted by several biodiscovery programs in the past. That said, many venomous animals are relatively small and deliver minuscule venom yields. Thus, the most commonly employed activity-guided biodiscovery pipeline cannot be applied effectively. Cell-free protein production may represent an attractive tool to produce selected venom components at high speed and without the creation of genetically modified organisms, promising rapid and highly efficient access to biomolecules for bioactivity studies. However, these methods have only sporadically been used in venom research and their potential remains to be established. Here, we explore the ability of a prokaryote-based cell-free system to produce a range of venom toxins of different types and from various source organisms. We show that only a very limited number of toxins could be expressed in small amounts. Paired with known problems to facilitate correct folding, our preliminary investigation underpins that venom-tailored cell-free systems probably need to be developed before this technology can be employed effectively in venom biodiscovery. Full article
(This article belongs to the Special Issue Versatility of Protein Synthesis in a Test Tube)
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