Synthetic biology (Oxford, England)最新文献

{"title":"Multicolor plate reader fluorescence calibration.","authors":"Jacob Beal,&nbsp;Cheryl A Telmer,&nbsp;Alejandro Vignoni,&nbsp;Yadira Boada,&nbsp;Geoff S Baldwin,&nbsp;Liam Hallett,&nbsp;Taeyang Lee,&nbsp;Vinoo Selvarajah,&nbsp;Sonja Billerbeck,&nbsp;Bradley Brown,&nbsp;Guo-Nan Cai,&nbsp;Liang Cai,&nbsp;Edward Eisenstein,&nbsp;Daisuke Kiga,&nbsp;David Ross,&nbsp;Nina Alperovich,&nbsp;Noah Sprent,&nbsp;Jaclyn Thompson,&nbsp;Eric M Young,&nbsp;Drew Endy,&nbsp;Traci Haddock-Angelli","doi":"10.1093/synbio/ysac010","DOIUrl":"https://doi.org/10.1093/synbio/ysac010","url":null,"abstract":"<p><p>Plate readers are commonly used to measure cell growth and fluorescence, yet the utility and reproducibility of plate reader data is limited by the fact that it is typically reported in arbitrary or relative units. We have previously established a robust serial dilution protocol for calibration of plate reader measurements of absorbance to estimated bacterial cell count and for green fluorescence from proteins expressed in bacterial cells to molecules of equivalent fluorescein. We now extend these protocols to calibration of red fluorescence to the sulforhodamine-101 fluorescent dye and blue fluorescence to Cascade Blue. Evaluating calibration efficacy via an interlaboratory study, we find that these calibrants do indeed provide comparable precision to the prior calibrants and that they enable effective cross-laboratory comparison of measurements of red and blue fluorescence from proteins expressed in bacterial cells.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysac010"},"PeriodicalIF":0.0,"publicationDate":"2022-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/71/0a/ysac010.PMC9357555.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40696991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Variability in cell-free expression reactions can impact qualitative genetic circuit characterization.","authors":"Katherine A Rhea,&nbsp;Nathan D McDonald,&nbsp;Stephanie D Cole,&nbsp;Vincent Noireaux,&nbsp;Matthew W Lux,&nbsp;Patricia E Buckley","doi":"10.1093/synbio/ysac011","DOIUrl":"https://doi.org/10.1093/synbio/ysac011","url":null,"abstract":"<p><p>Cell-free expression systems provide a suite of tools that are used in applications from sensing to biomanufacturing. One of these applications is genetic circuit prototyping, where the lack of cloning is required and a high degree of control over reaction components and conditions enables rapid testing of design candidates. Many studies have shown utility in the approach for characterizing genetic regulation elements, simple genetic circuit motifs, protein variants or metabolic pathways. However, variability in cell-free expression systems is a known challenge, whether between individuals, laboratories, instruments, or batches of materials. While the issue of variability has begun to be quantified and explored, little effort has been put into understanding the implications of this variability. For genetic circuit prototyping, it is unclear when and how significantly variability in reaction activity will impact qualitative assessments of genetic components, e.g. relative activity between promoters. Here, we explore this question by assessing DNA titrations of seven genetic circuits of increasing complexity using reaction conditions that ostensibly follow the same protocol but vary by person, instrument and material batch. Although the raw activities vary widely between the conditions, by normalizing within each circuit across conditions, reasonably consistent qualitative performance emerges for the simpler circuits. For the most complex case involving expression of three proteins, we observe a departure from this qualitative consistency, offering a provisional cautionary line where normal variability may disrupt reliable reuse of prototyping results. Our results also suggest that a previously described closed loop controller circuit may help to mitigate such variability, encouraging further work to design systems that are robust to variability. Graphical Abstract.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysac011"},"PeriodicalIF":0.0,"publicationDate":"2022-08-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9365049/pdf/ysac011.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40413432","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Signal amplification of <i>araC pBAD</i> using a standardized translation initiation region.","authors":"Patrick J Shilling,&nbsp;Diana Khananisho,&nbsp;Alister J Cumming,&nbsp;Bill Söderström,&nbsp;Daniel O Daley","doi":"10.1093/synbio/ysac009","DOIUrl":"https://doi.org/10.1093/synbio/ysac009","url":null,"abstract":"<p><p><i>araC pBAD</i> is a genetic fragment that regulates the expression of the <i>araBAD</i> operon in bacteria, which is required for the metabolism of L-arabinose. It is widely used in bioengineering applications because it can drive regulatable and titratable expression of genes and genetic pathways in microbial cell factories. A notable limitation of <i>araC pBAD</i> is that it generates a low signal when induced with high concentrations of L-arabinose (the maximum ON state). Herein we have amplified the maximum ON state of <i>araC pBAD</i> by coupling it to a synthetically evolved translation initiation region (<i>TIR^EVOL</i> ). The coupling maintains regulatable and titratable expression from <i>araC pBAD</i> and yet increases the maximal ON state by >5-fold. The general principle demonstrated in the study can be applied to amplify the signal from similar genetic modules. Graphical Abstract.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysac009"},"PeriodicalIF":0.0,"publicationDate":"2022-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/88/e2/ysac009.PMC9316229.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40556576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Traditional protocols and optimization methods lead to absent expression in a mycoplasma cell-free gene expression platform.","authors":"Andrei Sakai,&nbsp;Christopher R Deich,&nbsp;Frank H T Nelissen,&nbsp;Aafke J Jonker,&nbsp;Daniela M de C Bittencourt,&nbsp;Christopher P Kempes,&nbsp;Kim S Wise,&nbsp;Hans A Heus,&nbsp;Wilhelm T S Huck,&nbsp;Katarzyna P Adamala,&nbsp;John I Glass","doi":"10.1093/synbio/ysac008","DOIUrl":"https://doi.org/10.1093/synbio/ysac008","url":null,"abstract":"<p><p>Cell-free expression (CFE) systems are one of the main platforms for building synthetic cells. A major drawback is the orthogonality of cell-free systems across species. To generate a CFE system compatible with recently established minimal cell constructs, we attempted to optimize a <i>Mycoplasma</i> bacterium-based CFE system using lysates of the genome-minimized cell JCVI-syn3A (Syn3A) and its close phylogenetic relative <i>Mycoplasma capricolum</i> (Mcap). To produce mycoplasma-derived crude lysates, we systematically tested methods commonly used for bacteria, based on the S30 protocol of <i>Escherichia coli</i>. Unexpectedly, after numerous attempts to optimize lysate production methods or composition of feeding buffer, none of the Mcap or Syn3A lysates supported cell-free gene expression. Only modest levels of <i>in vitro</i> transcription of RNA aptamers were observed. While our experimental systems were intended to perform transcription and translation, our assays focused on RNA. Further investigations identified persistently high ribonuclease (RNase) activity in all lysates, despite removal of recognizable nucleases from the respective genomes and attempts to inhibit nuclease activities in assorted CFE preparations. An alternative method using digitonin to permeabilize the mycoplasma cell membrane produced a lysate with diminished RNase activity yet still was unable to support cell-free gene expression. We found that intact mycoplasma cells poisoned <i>E. coli</i> cell-free extracts by degrading ribosomal RNAs, indicating that the mycoplasma cells, even the minimal cell, have a surface-associated RNase activity. However, it is not clear which gene encodes the RNase. This work summarizes attempts to produce mycoplasma-based CFE and serves as a cautionary tale for researchers entering this field. Graphical Abstract.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysac008"},"PeriodicalIF":0.0,"publicationDate":"2022-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9239315/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40573536","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Highly efficient libraries design for saturation mutagenesis.","authors":"Gur Pines,&nbsp;Assaf Pines,&nbsp;Carrie A Eckert","doi":"10.1093/synbio/ysac006","DOIUrl":"https://doi.org/10.1093/synbio/ysac006","url":null,"abstract":"<p><p>Saturation mutagenesis is a semi-rational approach for protein engineering where sites are saturated either entirely or partially to include amino acids of interest. We previously reported on a codon compression algorithm, where a set of minimal degenerate codons are selected according to user-defined parameters such as the target organism, type of saturation and usage levels. Here, we communicate an addition to our web tool that considers the distance between the wild-type codon and the library, depending on its purpose. These forms of restricted collections further reduce library size, lowering downstream screening efforts or, in turn, allowing more comprehensive saturation of multiple sites. The library design tool can be accessed via http://www.dynamcc.com/dynamcc_d/. Graphical Abstract.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysac006"},"PeriodicalIF":0.0,"publicationDate":"2022-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/dd/d2/ysac006.PMC9205323.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40240035","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"SynBio2Easy-a biologist-friendly tool for batch operations on SBOL designs with Excel inputs.","authors":"Tomasz Zieliński, Johnny Hay, Andrew Romanowski, Anja Nenninger, Alistair McCormick, Andrew J Millar","doi":"10.1093/synbio/ysac002","DOIUrl":"10.1093/synbio/ysac002","url":null,"abstract":"<p><p>Practical delivery of Findable, Accessible, Reusable and Interoperable principles for research data management requires expertise, time resource, (meta)data standards and formats, software tools and public repositories. The Synthetic Biology Open Language (SBOL2) metadata standard enables FAIR sharing of the designs of synthetic biology constructs, notably in the repository of the SynBioHub platform. Large libraries of such constructs are increasingly easy to produce in practice, for example, in DNA foundries. However, manual curation of the equivalent libraries of designs remains cumbersome for a typical lab researcher, creating a barrier to data sharing. Here, we present a simple tool SynBio2Easy, which streamlines and automates operations on multiple Synthetic Biology Open Language (SBOL) designs using <i>Microsoft Excel®</i> tables as metadata inputs. The tool provides several utilities for manipulation of SBOL documents and interaction with SynBioHub: for example, generation of a library of plasmids based on an original design template, bulk deposition into SynBioHub, or annotation of existing SBOL component definitions with notes and authorship information. The tool was used to generate and deposit a collection of 3661 cyanobacterium <i>Synechocystis</i> plasmids into the public SynBioHub repository. In the process of developing the software and uploading these data, we evaluated some aspects of the SynBioHub platform and SBOL ecosystem, and we discuss proposals for improvement that could benefit the user community. With software such as SynBio2Easy, we aim to deliver a user-driven tooling to make FAIR a reality at all stages of the project lifecycle in synthetic biology research. Graphical Abstract.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":"7 1","pages":"ysac002"},"PeriodicalIF":2.6,"publicationDate":"2022-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8944294/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10841703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editing <i>Aspergillus terreus</i> using the CRISPR-Cas9 system.","authors":"Sra-Yh Shih,&nbsp;Uffe Hasbro Mortensen,&nbsp;Fang-Rong Chang,&nbsp;HsinYuan Tsai","doi":"10.1093/synbio/ysac031","DOIUrl":"https://doi.org/10.1093/synbio/ysac031","url":null,"abstract":"<p><p>CRISPR-Cas9 technology has been utilized in different organisms for targeted mutagenesis, offering a fast, precise and cheap approach to speed up molecular breeding and study of gene function. Until now, many researchers have established the demonstration of applying the CRISPR/Cas9 system to various fungal model species. However, there are very few guidelines available for CRISPR/Cas9 genome editing in <i>Aspergillus terreus</i>. In this study, we present CRISPR/Cas9 genome editing in <i>A. terreus</i>. To optimize the guide ribonucleic acid (gRNA) expression, we constructed a modified single-guide ribonucleic acid (sgRNA)/Cas9 expression plasmid. By co-transforming an sgRNA/Cas9 expression plasmid along with maker-free donor deoxyribonucleic acid (DNA), we precisely disrupted the <i>lovB</i> and <i>lovR</i> genes, respectively, and created targeted gene insertion (<i>lovF</i> gene) and iterative gene editing in <i>A. terreus</i> (<i>lovF</i> and <i>lovR</i> genes). Furthermore, co-delivering two sgRNA/Cas9 expression plasmids resulted in precise gene deletion (with donor DNA) in the <i>ku70</i> and <i>pyrG</i> genes, respectively, and efficient removal of the DNA between the two gRNA targeting sites (no donor DNA) in the <i>pyrG</i> gene. Our results showed that the CRISPR/Cas9 system is a powerful tool for precise genome editing in <i>A. terreus</i>, and our approach provides a great potential for manipulating targeted genes and contributions to gene functional study of <i>A. terreus</i>.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":"7 1","pages":"ysac031"},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/9e/24/ysac031.PMC9795164.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10454941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of an expression-tunable multiple protein synthesis system in cell-free reactions using T7-promoter-variant series.","authors":"Naoko Senda,&nbsp;Toshihiko Enomoto,&nbsp;Kenta Kihara,&nbsp;Naoki Yamashiro,&nbsp;Naosato Takagi,&nbsp;Daisuke Kiga,&nbsp;Hirokazu Nishida","doi":"10.1093/synbio/ysac029","DOIUrl":"https://doi.org/10.1093/synbio/ysac029","url":null,"abstract":"<p><p>New materials with a low environmental load are expected to be generated through synthetic biology. To widely utilize this technology, it is important to create cells with designed biological functions and to control the expression of multiple enzymes. In this study, we constructed a cell-free evaluation system for multiple protein expression, in which synthesis is controlled by T7 promoter variants. The expression of a single protein using the T7 promoter variants showed the expected variety in expression levels, as previously reported. We then examined the expression levels of multiple proteins that are simultaneously produced in a single well to determine whether they can be predicted from the promoter activity values, which were defined from the isolated protein expression levels. When the sum of messenger ribonucleic acid (mRNA) species is small, the experimental protein expression levels can be predicted from the promoter activities (graphical abstract (a)) due to low competition for ribosomes. In other words, by using combinations of T7 promoter variants, we successfully developed a cell-free multiple protein synthesis system with tunable expression. In the presence of large amounts of mRNA, competition for ribosomes becomes an issue (graphical abstract (b)). Accordingly, the translation level of each protein cannot be directly predicted from the promoter activities and is biased by the strength of the ribosome binding site (RBS); a weaker RBS is more affected by competition. Our study provides information regarding the regulated expression of multiple enzymes in synthetic biology.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":"7 1","pages":"ysac029"},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/fc/14/ysac029.PMC9791696.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10459894","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Self-growing environmentally responsive houses made from agricultural waste and fungal mycelia.","authors":"Sonja Billerbeck","doi":"10.1093/synbio/ysac003","DOIUrl":"https://doi.org/10.1093/synbio/ysac003","url":null,"abstract":"Mix the ingredients, pour them into a tin, and ‘bake’ at ambient temperature for 5days. What sounds like instructions for a ready-made baking mix could soon become a way to grow your own home—or emergency shelter needed after a natural disaster (1). While synthetic biology often focuses on using cells as factories to make molecules and nano-structures of interest, Rodrigo–Navarro et al focused on the cells themselves as the building blocks of macro-structure materials suitable for houses and shelters. This “engineered living material” (ELM) could be grown on demand, they are self-healing, responsive to environmental cues, and recyclable into new structures (2). This macro-scale ELM was developed in a collaboration between the New York-based biomaterial company Ecovative Design and the laboratories of Prof. Harris Wang (Columbia) and Prof. Chris Voigt. The ‘recipe’ for the team’s ELM requires a mix of agricultural byproducts, water, flour and calcium sulfate, and the tree fungus Ganoderma spec. The fungus uses the agricultural waste for nutrition and structural support. Once mixed and cast into brick-shaped foldable paper moulds, the fungal mycelia glue the agricultural waste together into a dense material. In contrast to Ecovative’s standard process of ‘baking’ the ingredients at high temperature, which kills the fungus, McBee et al were able to desiccate the material at ambient temperature. In this state, the fungus rests but can be revived by moisturization. This allows casting of modular bricks that can later be grown together into larger 3D structures—like walls or shelters—without additional mortar. It also allows the material to self-heal if broken. The authors show that a broken brick could be regrown by placing the broken halves close to each other with the healed material retaining most of its original mechanical properties. Further, the material could be fully recycled by grinding it down and using it as inoculum to grow new bricks. After developing this core living material, the team went one step further and equipped it with additional functions by adding an engineered bacterium that carries user-defined synthetic circuitry to the material mix. Instead of using an established, laboratory-tamed synthetic biology chassis such as Escherichia coli, which might have been outcompeted by the fungus, the authors performed a detailed microbiome analysis of the material, identifying and isolating a prevalent member, Pantoea agglomerans. They turned P. agglomerans into an engineerable chassis that could be reintroduced and maintained within the material. The authors then implemented a toy circuit distributed over two engineered strains of P. agglomerans. The first strain generated a volatile quorum sensing molecule (sender strain) that could be sensed and propagated through the material by a second strain (responderpropagator strain) that also created a fluorescent output that could be visualized under the microscope. As such, individual bricks ","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":"7 1","pages":"ysac003"},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9845837/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10579566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cofactor-independent RNA editing by a synthetic S-type PPR protein.","authors":"Kalia Bernath-Levin,&nbsp;Jason Schmidberger,&nbsp;Suvi Honkanen,&nbsp;Bernard Gutmann,&nbsp;Yueming Kelly Sun,&nbsp;Anuradha Pullakhandam,&nbsp;Catherine Colas des Francs-Small,&nbsp;Charles S Bond,&nbsp;Ian Small","doi":"10.1093/synbio/ysab034","DOIUrl":"https://doi.org/10.1093/synbio/ysab034","url":null,"abstract":"<p><p>Pentatricopeptide repeat (PPR) proteins are RNA-binding proteins that are attractive tools for RNA processing in synthetic biology applications given their modular structure and ease of design. Several distinct types of motifs have been described from natural PPR proteins, but almost all work so far with synthetic PPR proteins has focused on the most widespread P-type motifs. We have investigated synthetic PPR proteins based on tandem repeats of the more compact S-type PPR motif found in plant organellar RNA editing factors and particularly prevalent in the lycophyte <i>Selaginella</i>. With the aid of a novel plate-based screening method, we show that synthetic S-type PPR proteins are easy to design and bind with high affinity and specificity and are functional in a wide range of pH, salt and temperature conditions. We find that they outperform a synthetic P-type PPR scaffold in many situations. We designed an S-type editing factor to edit an RNA target in <i>E. coli</i> and demonstrate that it edits effectively without requiring any additional cofactors to be added to the system. These qualities make S-type PPR scaffolds ideal for developing new RNA processing tools.</p>","PeriodicalId":74902,"journal":{"name":"Synthetic biology (Oxford, England)","volume":" ","pages":"ysab034"},"PeriodicalIF":0.0,"publicationDate":"2021-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8809517/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39757488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}