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This advancement, published in Nature, describes the creation of a genomically recoded organism (GRO) named 'Ochre'. It uses a single stop codon, enabling the production of synthetic proteins with innovative properties. These proteins could revolutionize biotherapies and biomaterials.
The scientists compressed redundant codons into a single one, thereby freeing up codons for new functions. This feat relies on over 1,000 precise modifications of the genome, an unprecedented achievement in genomic engineering.
Farren Isaacs and Jesse Rinehart, co-authors of the study, emphasize the importance of this technological platform. It not only allows exploration of the malleability of genetic codes but also the development of industrial applications beneficial to society.
Michael Grome, the study's lead author, compares codons to words in a genetic recipe. By eliminating two of the three stop codons, the researchers were able to assign new functions to these codons, allowing the incorporation of non-standard amino acids into proteins.
This research builds on previous work published in Science in 2013. It represents a significant step towards creating a non-redundant genetic code in E. coli, an ideal organism for the production of synthetic proteins.
The potential applications of this technology are vast, ranging from reducing undesirable immune responses to improving the conductivity of biomaterials. Isaacs and Rinehart are collaborating with Pear Bio, a Yale spin-off, to commercialize these programmable biologics.
This study marks a turning point in our ability to manipulate the genetic code for medical and industrial applications. It paves the way for a new generation of biotherapies and biomaterials, with profound implications for human health and biotechnology.
What is a codon and how does it work?
A codon is a sequence of three nucleotides in DNA or RNA that codes for a specific amino acid, serving as a building block for proteins. There are 64 different codons, with 61 coding for the 20 natural amino acids, and three serving as stop codons, signaling the end of protein synthesis.
Codons function as instructions in the translation process, where genetic information is converted into proteins. Each codon corresponds to a specific amino acid, and the order of codons in a gene determines the order of amino acids in the resulting protein.
The redundancy of the genetic code means that multiple codons can code for the same amino acid. This redundancy offers some flexibility and resilience to the genetic code, allowing for silent mutations that do not change the amino acid sequence of the protein.
In this study, the researchers exploited this redundancy to recode the genome of an organism, compressing redundant codons into a single one and reassigning the freed codons to new functions, such as incorporating non-standard amino acids into proteins.
What are the potential applications of synthetic proteins?
Synthetic proteins, produced through genomically recoded organisms like 'Ochre', open the door to numerous applications in medicine and biotechnology. These proteins can be designed to have unique properties.
In the medical field, synthetic proteins could be used to develop new biologic drugs with reduced side effects. For example, by incorporating non-standard amino acids, researchers can create proteins that are less likely to trigger an undesirable immune response in patients.
In industry, synthetic proteins could be used to create biomaterials with enhanced properties, such as improved electrical conductivity or increased resistance. These materials could have applications in fields ranging from electronics to construction.
Finally, this technology could also be used to explore fundamental questions in biology, such as the malleability of the genetic code and the limits of life as we know it. By pushing these boundaries, researchers could discover new pathways for protein synthesis and organism design.