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• W3159181194 abstract "Summary Protein translation using four-base codons occurs in both natural and synthetic systems. What constraints contributed to the universal adoption of a triplet-codon, rather than quadruplet-codon, genetic code? Here, we investigate the tolerance of the E. coli genetic code to tRNA mutations that increase codon size. We found that tRNAs from all twenty canonical isoacceptor classes can be converted to functional quadruplet tRNAs (qtRNAs), many of which selectively incorporate a single amino acid in response to a specified four-base codon. However, efficient quadruplet codon translation often requires multiple tRNA mutations, potentially constraining evolution. Moreover, while tRNAs were largely amenable to quadruplet conversion, only nine of the twenty aminoacyl tRNA synthetases tolerate quadruplet anticodons. These constitute a functional and mutually orthogonal set, but one that sharply limits the chemical alphabet available to a nascent all-quadruplet code. Our results illuminate factors that led to selection and maintenance of triplet codons in primordial Earth and provide a blueprint for synthetic biologists to deliberately engineer an all-quadruplet expanded genetic code." @default.
• W3159181194 created "2021-05-10" @default.
• W3159181194 creator A5063338821 @default.
• W3159181194 creator A5063450287 @default.
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• W3159181194 date "2021-04-26" @default.
• W3159181194 modified "2023-09-23" @default.
• W3159181194 title "Measuring the tolerance of the genetic code to altered codon size" @default.
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• W3159181194 doi "https://doi.org/10.1101/2021.04.26.441066" @default.
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