%0 Journal Article %1 Lajoie2013Genomically %A Lajoie, Marc J. %A Rovner, Alexis J. %A Goodman, Daniel B. %A Aerni, Hans-Rudolf %A Haimovich, Adrian D. %A Kuznetsov, Gleb %A Mercer, Jaron A. %A Wang, Harris H. %A Carr, Peter A. %A Mosberg, Joshua A. %A Rohland, Nadin %A Schultz, Peter G. %A Jacobson, Joseph M. %A Rinehart, Jesse %A Church, George M. %A Isaacs, Farren J. %D 2013 %I American Association for the Advancement of Science %J Science %K synthetic-biology translation %N 6156 %P 357--360 %R 10.1126/science.1241459 %T Genomically Recoded Organisms Expand Biological Functions %U http://dx.doi.org/10.1126/science.1241459 %V 342 %X Easily and efficiently expanding the genetic code could provide tools to genome engineers with broad applications in medicine, energy, agriculture, and environmental safety. Lajoie et al. (p. 357) replaced all known UAG stop codons with synonymous UAA stop codons in Escherichia coli MG1655, as well as release factor 1 (RF1; terminates translation at UAG), thereby eliminating natural UAG translation function without impairing fitness. This made it possible to reassign UAG as a dedicated codon to genetically encode nonstandard amino acids while avoiding deleterious incorporation at native UAG positions. The engineered E. coli incorporated nonstandard amino acids into its proteins and showed enhanced resistance to bacteriophage T7. In a second paper, Lajoie et al. (p. 361) demonstrated the recoding of 13 codons in 42 highly expressed essential genes in E. coli. Codon usage was malleable, but synonymous codons occasionally were nonequivalent in unpredictable ways.

@article{Lajoie2013Genomically, abstract = {Easily and efficiently expanding the genetic code could provide tools to genome engineers with broad applications in medicine, energy, agriculture, and environmental safety. Lajoie et al. (p. 357) replaced all known {UAG} stop codons with synonymous {UAA} stop codons in Escherichia coli {MG1655}, as well as release factor 1 ({RF1}; terminates translation at {UAG}), thereby eliminating natural {UAG} translation function without impairing fitness. This made it possible to reassign {UAG} as a dedicated codon to genetically encode nonstandard amino acids while avoiding deleterious incorporation at native {UAG} positions. The engineered E. coli incorporated nonstandard amino acids into its proteins and showed enhanced resistance to bacteriophage T7. In a second paper, Lajoie et al. (p. 361) demonstrated the recoding of 13 codons in 42 highly expressed essential genes in E. coli. Codon usage was malleable, but synonymous codons occasionally were nonequivalent in unpredictable ways.}, added-at = {2018-12-02T16:09:07.000+0100}, author = {Lajoie, Marc J. and Rovner, Alexis J. and Goodman, Daniel B. and Aerni, Hans-Rudolf and Haimovich, Adrian D. and Kuznetsov, Gleb and Mercer, Jaron A. and Wang, Harris H. and Carr, Peter A. and Mosberg, Joshua A. and Rohland, Nadin and Schultz, Peter G. and Jacobson, Joseph M. and Rinehart, Jesse and Church, George M. and Isaacs, Farren J.}, biburl = {https://www.bibsonomy.org/bibtex/247750710ace474118a82074a05ba65de/karthikraman}, citeulike-article-id = {12735464}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1241459}, citeulike-linkout-1 = {http://www.sciencemag.org/content/342/6156/357.abstract}, citeulike-linkout-2 = {http://www.sciencemag.org/content/342/6156/357.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/24136966}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=24136966}, day = 18, doi = {10.1126/science.1241459}, interhash = {57c1f2c651934f301d574f74ad7c4dfb}, intrahash = {47750710ace474118a82074a05ba65de}, issn = {1095-9203}, journal = {Science}, keywords = {synthetic-biology translation}, month = oct, number = 6156, pages = {357--360}, pmid = {24136966}, posted-at = {2013-11-01 08:05:59}, priority = {2}, publisher = {American Association for the Advancement of Science}, timestamp = {2018-12-02T16:09:07.000+0100}, title = {Genomically Recoded Organisms Expand Biological Functions}, url = {http://dx.doi.org/10.1126/science.1241459}, volume = 342, year = 2013 }