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Expanding and reprogramming the genetic code

Author

Listed:
  • Jason W. Chin

    (Medical Research Council Laboratory of Molecular Biology
    Cambridge University)

Abstract

Nature uses a limited, conservative set of amino acids to synthesize proteins. The ability to genetically encode an expanded set of building blocks with new chemical and physical properties is transforming the study, manipulation and evolution of proteins, and is enabling diverse applications, including approaches to probe, image and control protein function, and to precisely engineer therapeutics. Underpinning this transformation are strategies to engineer and rewire translation. Emerging strategies aim to reprogram the genetic code so that noncanonical biopolymers can be synthesized and evolved, and to test the limits of our ability to engineer the translational machinery and systematically recode genomes.

Suggested Citation

  • Jason W. Chin, 2017. "Expanding and reprogramming the genetic code," Nature, Nature, vol. 550(7674), pages 53-60, October.
    • Handle: RePEc:nat:nature:v:550:y:2017:i:7674:d:10.1038_nature24031
    DOI: 10.1038/nature24031
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    Cited by:

    1. Haoran Huang & Tao Yan & Chang Liu & Yuxiang Lu & Zhigang Wu & Xingchu Wang & Jie Wang, 2024. "Genetically encoded Nδ-vinyl histidine for the evolution of enzyme catalytic center," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Antje Krüger & Andrew M. Watkins & Roger Wellington-Oguri & Jonathan Romano & Camila Kofman & Alysse DeFoe & Yejun Kim & Jeff Anderson-Lee & Eli Fisker & Jill Townley & Anne E. d’Aquino & Rhiju Das & , 2023. "Community science designed ribosomes with beneficial phenotypes," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    3. Hongxia Zhao & Wenlong Ding & Jia Zang & Yang Yang & Chao Liu & Linzhen Hu & Yulin Chen & Guanglong Liu & Yu Fang & Ying Yuan & Shixian Lin, 2021. "Directed-evolution of translation system for efficient unnatural amino acids incorporation and generalizable synthetic auxotroph construction," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    4. Yiman Gao & Jie Liu & Cong Wei & Yan Li & Kui Zhang & Liangliang Song & Lingchao Cai, 2022. "Photoinduced β-fragmentation of aliphatic alcohol derivatives for forging C–C bonds," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    5. Yuda Chen & Shikai Jin & Mengxi Zhang & Yu Hu & Kuan-Lin Wu & Anna Chung & Shichao Wang & Zeru Tian & Yixian Wang & Peter G. Wolynes & Han Xiao, 2022. "Unleashing the potential of noncanonical amino acid biosynthesis to create cells with precision tyrosine sulfation," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    6. Vaitea Opuu & Giuliano Nigro & Thomas Gaillard & Emmanuelle Schmitt & Yves Mechulam & Thomas Simonson, 2020. "Adaptive landscape flattening allows the design of both enzyme: Substrate binding and catalytic power," PLOS Computational Biology, Public Library of Science, vol. 16(1), pages 1-19, January.
    7. Joongoo Lee & Jaime N. Coronado & Namjin Cho & Jongdoo Lim & Brandon M. Hosford & Sangwon Seo & Do Soon Kim & Camila Kofman & Jeffrey S. Moore & Andrew D. Ellington & Eric V. Anslyn & Michael C. Jewet, 2022. "Ribosome-mediated biosynthesis of pyridazinone oligomers in vitro," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    8. Huan Sun & Haiyang Jia & Olivia Kendall & Jovan Dragelj & Vladimir Kubyshkin & Tobias Baumann & Maria-Andrea Mroginski & Petra Schwille & Nediljko Budisa, 2022. "Halogenation of tyrosine perturbs large-scale protein self-organization," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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